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Stabilisation of Curcumin for Delivery Inside Live Cell
Md Asif Amin
Department of Chemistry, Suri Vidyasagar College, Suri-731101, WB, India.
DOI:
https://doi.org/10.51583/IJLTEMAS.2026.150400044
Received: 10 April 2026; Accepted: 15 April 2026; Published: 06 May 2026
ABSTRACT
Curcumin, widely used as spice in Asia is found in rhizome of turmeric plant (Curcuma longa and Curcuma
xanthorrhiza). It shows antibacterial, anti-inflammatory, hypoglycemic, antioxidant, antimicrobial activities and
capable of treating fatal disease like cancer, Parkinson’s disease. It is highly unstable in aqueous solution
specially in high pH condition makes it deceptively useful. In this this review we have shown several techniques
and schemes that made curcumin a potent useful drug. Forming complex with proteins, lipids, lipoproteins,
cyclodextrin and bio-mimicking molecules is effective to increase bioavailability of this hydrophobic molecule.
Nature of interactions and binding mechanism with those molecules are discussed here. Most important aspect
of this review is to deliver curcumin inside live cells and finding the effects on cell death (apoptosis) and
proliferations. Different drug delivery systems have been developed which show excellent rate of internalisation.
Curcumin has been delivered intravenously in live mouse model.
Keywords: Curcumin, Internalisation, Bio availability, Drug delivery, Proliferation
INTRODUCTION
Drugs from natural sources become a matter of great interest in drug research. Natural drugs are prior over
synthetic drugs because of hazard in synthesis, stereo-speficic conformation. The working principal of those
drugs depends on the method of intake. Effectiveness depends on the selective delivery to the affected region
and functionality after delivery. Rhizomes of Curcuma longa (turmeric) are used from the early days for
treatment of various diseases as it has anti-inflammatory, antimicrobial, and anti-carcinogenic properties.
1-6
From long ago curcumin is used to protect from sun burns and also to prevent any skin ailments like leuco-
derma etc. It exhibits strong antioxidant properties, which have been validated through various in vitro and in
vivo tests.
7-11
It has been studied for its potential therapeutic effects in neurological disorders such as
Alzheimer's, Parkinson's, and Huntington's diseases. Its low cost, ability to cross the blood-brain barrier, and
pharmacological safety, as demonstrated in preclinical studies, suggest it may play a beneficial role in managing
these conditions.
12-16
Despite all of these it has low bioavailability and poor pharmacokinetics due to its low
solubility and rapid degradation at aqueous media as well as physiological pH.
17
For these it has poor in vivo
efficacy.
18
Phase I and Phase II trials with curcumin administered alone orally was done with high concentration
of drugs
19-20
. While, there are also review articles describing photo physical, photochemical properties along
with application in nano and biological systems,
21-22
here we primarily focused on various destabilisation factors
of curcumin and strategy those overcome the destabilisation factors in physiological conditions. Moreover we
have pointed out some important techniques of developing drug delivery systems to deliver curcumin inside live
cell. Those delivery vehicle increased extent of internalisation of curcumin inside live cell. The conjugates
showed excellent rate of cancer cell death and inhibit proliferation of malignant cells with low dosage
concentration in comparison to curcumin alone as curcumin is unstable in biological aqueous medium (biological
water). Different cancer cell needs different curcumin delivery systems as they differs in properties.
Increasing bioavailability of Curcumin by formation of stable complex with bio-mimicking Systems:
Curcumin posses potent nuclear factor-kappaB (NF-kappaB) and tumor inhibitory properties can not show
biological effectiveness due to its poor water solubility and high degradability under neutral and alkaline
medium. In neutral basic conditions structure of curcumin degraded as proton removed from phenolic group. In
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this condition curcumin degraded to trans-6-(4'-hydroxy-3'-methoxyphenyl)-2,4-dioxo-5-hexenal as major
product and vanillin, ferric acid, feruloyl methane as minor product and hence it is almost non-fluorescent in
aqueous medium
17
. However, people made efforts to increase the bioavailability of curcumin after loading into
different self-assembled ordered bioactive systems like micelles, microemulsions, vesicles, proteins, and
cyclodextrins. Bera et al prepared sorbitan monoesters (Span 20 and Span 80) assisted giant vesicles employing
an imidazolium surface active ionic liquid (SAIL), 1-hexadecyl-3-methylimida- zolium chloride ([C16mim]Cl),
in an aqueous medium. Curcumin became stable in the micellar and giant vesicular assemblies of [C16mim]Cl
and Sorbitan mono-esters and showed fluorescence. They are the first group to perform ultrafast solvation
dynamics (femtosecond fluorescence up-conversion) of curcumin in different vesicular aggregates and got three
distinct lifetime components from fluorescence up-conversion decay. Two slow components attributed to
solvation dynamics and slow component arises due to excited state intramolecular hydrogen atom transfer
(ESIHT) due to keto-enol tautomerism. From the life time component of micellar and vesicle media they also
proved that Span 80 possesses more rigid environment than span 20
23
. Mandal et al prepared niosomes from
non-ionic Tween-20 micelles and Tween-20/cholesterol. Phospholipid like structural environment of niosomes
can be a host of hydrophobic molecule like curcumin and may be a righteous drug delivery system. Curcumin
got stability in niosomes owing to of H bond interactions with both the oxyethylene functionality of Tween-20
and hydroxyl functionality of cholesterol
24
.
Encapsulation with Cyclodextrin and its derivative
Yallapu and co-workers developed a cyclodextrin (CD) mediated curcumin drug delivery system via
encapsulation technique. Curcumin encapsulation into the CD cavity was achieved by inclusion complex
mechanism and encapsulation efficiency was improved by increasing the ratio of curcumin to CD.
25
Kee and co
workers showed two diamide (either a succinamide (su) or a urea (ur) linker) linked γ-CD dimers successfully
inhibited degradation of curcumin in aqueous medium at pH 7.4 and 37º C. Curcumin forms 1:1 cooperative
association with 66γCD2su and 66γCD2ur and with curcumin occupying both γ-CD annuli (as shown in Figure
1) evident from 2D
1
H NOESY NMR data. This association may be a potential drug delivery system to
membranes and furthermore to the intracellular milieu. Using fluorescence quantum yield as a marker they
proved the associations are proficient to deliver curcumin to a model membrane system of micelles consist of
sodium dodecyl sulfate (SDS)
26
. They have also studied excited state dynamics of curcumin complexed with
66γCD2su and 66γCD2ur using femtosecond transient absorption spectroscopy and reveal solvent reorganisation
and ESIHT dynamics. Growth component attributed to rapid solvent reorganisation and fast decay component
(among three decay components) was assigned as relaxation due to ESIHT dynamics. Whereas other two
relatively slow decay components with small amplitude appeared due to dynamics of complexed curcumin and
molecular motions due to flexibility of the γ-CD moieties
27
. In another work curcumin is protected from
hydrophilic environment by its microencapsulation in hydroxypropyl-β-cyclodextrin. Then silver nanoparticles
was synthesized using curcumin: cyclodextrin complex in aqueous medium and loaded them into bacterial
cellulose hydrogel to get moist wound-healing properties. The cytocompatible hydrogel showed broad-spectrum
antimicrobial activity along with antioxidant properties against three common wound-infecting pathogenic
microbes Staphylococcus aureus, Pseudomonas aeruginosa, and Candida auris.
28
Figure 1. Structures of (a) curcumin, (b) γ-CD, and curcumin complexed with (c) 66γCD2su and (d) 66γCD2ur. Reproduced with permission from
ACS
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Stabilisation of curcumin by forming conjugate with protein
For any drug, one of the most important aspect is the interaction of the drug with different components of blood.
So many people investigated the interaction of curcumin with HSA as it is a important factor that determine
toxicity and therapeutic dosage. Zsila and coworkers showed that Cyclic dichroism (CD) of HSA- curcumin
complex has pH dependent biphasic band in visible region. Asymmetric environment of HSA made 𝛑-𝛑
*
transition of curcumin optically active. The complex possesed three bands, positive at 485 nm and negatives at
423 nm and 368 nm with crossover point at 445 nm. Negative Cotton effect at shorter wavelength observed in
visible absorption spectra due to dissymmetric conformation of the curcumin molecule upon binding to HSA. It
confirms mutual rotations of the two feruloyl moieties around the central methylene group allowing
intramolecular exciton coupling between their electronic transition moments
29
. In order to get molecular basis
of the Cotton effects induced by the binding of curcumin to human serum albumin they have done semiempirical
calculations by Gaussian 98 program using AM1 method and found that curcumin binds near the single
tryptophan residue of HSA in a right-handed conformation stabilized by a number of basic amino acids able to
form intermolecular hydrogen bonds.
30
Researchers also investigated effect of curcumin on binding of other drug (tamoxifen) with HSA with the help
of steady state fluorescence spectroscopy. When two drugs applied together competition between them can
decrease binding fraction of tamoxifen with concomitant increase in concentration of free tamoxifen. Binding of
tamoxifen and curcumin with HSA can be confirmed by fluorescence quenching study. The binding sites of HSA
are hydrophobic subdomains IIA (Trp 214 and Tyr 263), IB (Tyr 138, Tyr 140, Tyr 148, Tyr 150, Tyr 160) and
IIIA (Tyr 401, Tyr 411, Tyr 497) as major of the fluorescence of HSA arises due to tryptophan and tyrosyl
residues located at those sub domains
31
. Patra et al suggested a simultaneous static and dynamic fluorescence
quenching mechanism operating in the complex formation between HSA and curcumin. Two fold increase in
rate of depletion of synchronous fluorescence spectra (SFS) intensity for tryptophan with respect to tyrosine in
HSA in SFS spectrum also indicated that curcumin is located at close proximity of tryptophan. They also
observed that curcumin remain bounded to unfolded state of HSA and facilitated the process by pushing
tryptophan moiety to more polar environment in the unfolded state. From the k
q
values they concluded like native
form, curcuminHSA complex is formed in the unfolded and refolded states
32
.
Leung et al explain the observation curcumin is stabilized at the wound site to enable healing despite of blood
plasma is composed of approximately 92% water and found the factor that stabilised curcumin. They investigate
the effect of major plasma proteins(specifically on effect of hydrolysis of curcumin at pH 7.4), which include
human serum albumin (HSA), fibrinogen, immunoglobulin G (IgG), and transferrin, on stabilization of
curcumin. The hydrolysis was rapid in presence of transferrin and IgG and the reaction is suppressed in presence
of either HSA or fibrinogen with an impressive yield of approximately 95%. They also calculated the binding
constants of curcumin to HSA and fibrinogen are on the order of 10
4
M
-1
and 10
5
M
-1
, respectively. It was
established that degradation of curcumin can be inhibited by presence of HSA and fibrinogen due to strong
interaction
33
. Using various interaction with proteins curcumin may be used for treatment of Parkinson’s disease
(PD) and other neurological diseases. In PD oligomerization and amyloid formation of α-synuclein (α-Syn)
causes the toxicity. Curcumin does not bind to monomeric α-Syn but binds specifically to oligomeric
intermediates which has been supported by fluorescence and two-dimensional nuclear magnetic resonance (2D-
NMR) studies. Beside this, curcumin accelerates formation of less toxic, ordered structure (fibril) of α-Syn by
binding with preformed oligomers and fibrils and altering their hydrophobic surface exposure
34
.
Delivery of curcumin inside cell
The natural pigment curcumin is hydrophobic in nature. So, curcumin needs a carrier system to be delivered
inside cell. For this purpose Kunwar et al observed the interaction of curcumin with two biologically important
transport systems, liposomes, phosphatidylcholine (PC) and human serum albumin (HSA). Curcumin does not
exhibit fluorescence in aqueous solution. Its fluorescence quantum yield and fluorescence maximum are
sensitive to solvent polarity and protic nature of the solvent. Using this property, as a monitor of interaction with
biomolecules, they have found average binding constants of curcumin to PC and HSA were estimated to be 2.5
× 10
4
M
-1
and 6.1 × 10
4
M
-1
respectively. Cellular uptake studies was done using both delivery vehicle liposomes
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and HSA for two cell lines, normal mouse lymphocytes and mouse T lymphoma cell line EL4. The amount of
cellular uptake was evaluated by measuring absorbance of methanol extracted cell lysate as a function of the
total amount of curcumin added in the incubation medium. HSA delivered curcumin endogenously where else
liposome delivered exogenously and most important observation was lymphoma cell showed preferential uptake
of curcumin over normal cells.
35
Fatemizadeh et al used optimised niosomal formulation for co-delivery of tamoxifen and curcumin and showed
that niosomal nanoparticle can reduce the side effects of drugs inside normal cell
36
.
Kee and co workers reported
intracellular delivery of curcumin inside human prostate cancer cells (PC-3) using 66γCD2su and 66γCD2ur as
delivery agents (see section 2.2). 66γCD2su and 66γCD2ur are nontoxic toward PC-3 cell as these delivery
agents did not affect cellular proliferation or death and their diamine linker were being hydrolyzed enzymatically
in the cellular environment. Whereas curcumin inhibited proliferation of PC-3 cells in a dose dependent manner
which is confirmed by trypan blue exclusion studies using confocal fluorescence imaging, uptake studies with
fluorescence spectroscopy. Those observations were also confirmed by expression of curcumin target genes
37
.
Priyadarsini group quantitatively calculated cellular uptake of curcumin using absorption and fluorescence
spectroscopy in two types of normal cells: spleen lymphocytes, and NIH3T3 and two tumor cell lines: EL4 and
MCF7. Malignant cells took up more curcumin than normal cell lines and fluorescence intensities inside cancer
cells were higher compared to normal cells. Differential localization of curcumin in the membrane, cytoplasm
and nuclear compartments of the cell with preferred localization in the membrane was observed from
fluorescence imaging and studies on isolation of curcumin from sub-cellular fractions. Cytotoxicity experiment
had also done at 20 and 40 nmol/ml in different cell lines. Higher cytotoxicity are observed in cancer cells but
there is no general correlation between uptake and toxicity
38
. Safavi et al made conjugate of curcumin with two
different sized polyethylene glycol (PEG) to overcome low aqueous solubility and destabilisation of curcumin.
PEG is hydrophilic, biocompatible and were covalently attached to the drug through a urethane linkage with 1:1
CCMN/PEG molar ratios. The conjugate were able to show more cytotoxicity in PC-3 (human pancreatic
carcinoma) cells than free curcumin
39
.
People also made an attempt to deliver curcumin into tissue macrophages through intravenous injection by
formulation of curcumin embedded phospholipid vesicles or lipid-nanospheres. For this purpose rat animal
model was studied (n=5) and response of blood cells along with drug distribution to different organ was
observed. White blood cells (WBC), red blood cells (RBC) and platelets (PLT) tended to decrease and then
returned to baseline. Concomitant yellow fluorescence in the confocal scanning microscopy images from bone
marrow, liver, and spleen samples confirmed delivery of curcumin in those organs
40
. Curcumin-based ionic
liquid hydrogel loaded with ilomastat (Cur-Car-IL@Ilo hydrogel) is also effective in sustained release of drugs
and improve the skin permeability of drugs in mice with significantly reduced expression levels of inflammatory
factors, matrix metalloproteinase 8, and collagen-I. Content of anaerotruncus, proteus, and UCG-009 bacteria in
the gut of psoriatic mice increased supported by flora analysis with concomitant decrease of the expressions of
iron death-related proteins SLC7A11 and ASL4 significantly after treatment with Cur-Car-IL@Ilo hydrogel
41
.
However, water soluble composite of curcumin is highly demanding for biological applications. Mukherjee and
coworker synthesised tetrafacial water-soluble molecular barrel (1) by coordination driven self-assembly of a
symmetrical tetrapyridyl donor (L) with a cis-blocked 90° acceptor [cis-(en)Pd(NO3)2] (en = ethane-1,2-
diamine) of which hydrophobic cavity encapsulated curcumin. This complex was used as carrier to transport
curcumin inside human prostate cancer cell line HeLa
42
.
Nanostructures mediated curcumin delivery inside live cell:
Bisht et al synthesized cross linked polymer nanoparticles of N-isopropylacrylamide (NIPAAM), N-vinyl-2-
pyrrolidinone (VP) and poly(ethyleneglycol) acrylate (PEG-A) as delivery agent of curcumin. These nano
carriers are ideal for study of effects of hydrophobic drugs as these are nontoxic proved by both in vivo and in
vitro experiments. Nanocurcumin formed after binding with these polymeric nanoparticles and efficiency
increased with respect to free curcumin against pancreatic cancer cell lines in vitro, by inhibiting cell viability
and colony formation in soft agar. However, the mechanism of specificity of nano form is same as free curcumin,
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inhibiting the activation of the seminal transcription factor NFκB, and reducing steady state levels of pro-
inflammatory cytokines like interleukins and TNFα
43
. Using low-temperature (LT) method Yadava et al
prepared curcumin (CMN)-loaded nanostructure hybrid lipid capsules (CMN-nHLCs) of three sizes (25, 75, and
150 nm) with 4% (w/w) loading capacity. It showed long term storage stability at 4 ºC and controlled release of
CMN from nHLCs at 37 °C showed anticancer efficacy compared to free CMN in breast cancer cells (non-
bCSCs) and breast cancer stem-like cells (bCSCs). Significant reduction in their mammosphere size/number and
stemness was observed on internalization of CMN-nHLCs into MCF-7 cells (non-bCSCs and bCSCs)
44
.
Patra et al loaded curcumin on solid lipid nanoparticles (SLNs) derived from S-(−)-γ-amino-α-hydroxybutyric
acid (GAHBA), γ-aminobutyric acid (GABA). They optimised the formulation based on the stability, particle
size, and polydispersity and reached at greater curcumin entrapment efficiency of the SLNs. Enhanced rate of
drug release from curcumin-loaded SLNs consisting of the lipid containing−OH groups at the lipid head induced
cell death in a concentration-dependent manner in both human prostatic adenocarcinoma PC 3 cell line and
human breast carcinoma MCF7 cell line
45
. Diblock dendrosome nanopolymer (OM200) was used to formulated
curcumin and tamoxifen to increase efficacy of the drug against tamoxifen-resistant (TR) metastatic breast
cancer (MCF-7) cells. Most significantly the formulation is non toxic to normal breast fibroblast cells
46
. Another
group also synthesized mannose surface-modified solid lipid nanoparticles (SLNs) loaded with curcumin (Man-
CUR SLN) which showed inhibitory effects on lung cancer cell (A549) migration and proliferation. Higher
cellular uptake and delivery was also confirmed by confocal microscope study (Figure 6). Improved
encapsulation efficiency and drug release capacity of Man-CUR SLN showed antibacterial effects against
Mycobacterium intracellulare (M.i.) and M.i.-infected macrophages
47
.
Figure 6: (A) FT-IR spectrum showing a specific mannose peak for Man-CUR SLNs. (B) Comparison of in
vitro drug release rates of free CUR and Man-CUR SLNs. (C) Fluorescence spectra of bare SLNs and CUR-
SLNs. CUR-SLNs exhibit a specific peak between 500 and 600 nm. (D) Confocal microscopy images
illustrating the cellular uptake of CUR and SLNs in A549 lung cancer cells. Notably, the Man-CUR SLNs
exhibit a substantially stronger green fluorescence signal than does free CUR. CUR, curcumin; FT-IR, Fourier
transform infrared; Man-CUR SLN; mannose surface-modified solid lipid nanoparticles loaded with curcumin;
and SLNs, solid lipid nanoparticles. Reproduced with permission from ACS
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Nanocurcumin prepared by sol-oil method could improve absorption and bioavailability towards human
laryngeal cancer cell line (Hep-2). Apoptosis detection methods (Annexin V/PI staining, AO/EB staining, and
comet assays), flow cytometric analyses and gene expression studies, suggested significant inhibition effects
against the proliferation of Hep-2 cells through G2/M cell cycle arrest and the induction of apoptosis, which was
dependent on Caspase-3 and p53 activation
48
. Guo et al developed implantable curcumin-loaded poly(ε-
caprolactone)-poly(ethylene glycol)-poly-caprolactone) (PCL-PEG-PCL, PCEC) nanofibers by
electrospinning method. Curcumin-loaded fibers showed antitumor activity against rat Glioma 9L cells for
prolonged period whereas antitumor activity of pure curcumin disappeared within 48 h and PCEC fibers non
toxic towards Glioma 9L cells (cell growth is unaffected)
49
. Another group synthesised CUR-loaded polyvinyl
pyrrolidone (CUR@PVP) nanofibers via electrospinning which are quickly dissolved in phosphate-buffered
saline (PBS) solution. X-ray diffraction (XRD) and FTIR revealed that CUR was evenly distributed in the
nanofibers by formation of hydrogen bond between cur cumin and polymer matrix. Nanosolid dispersion system
increased the bioavailability in B16 cell line (in vitro) and also in animal model of rat (in vivo) which increased
anticancer effect
50
.
S.No
Types of Delivery System/ Conjugate
1
liposomes, phosphatidylcholine (PC) and
human serum albumin (HSA).
2
Noisome for co-delivery of tamoxifen and
curcumin
3
66γCD2su and 66γCD2ur
4
DMSO and diluted by culture medium
5
Polyethyleneglycol(PEG)
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S.No
Types of Delivery System/ Conjugate
6
cross linked polymer nanoparticles of N-
isopropylacrylamide (NIPAAM), N-
vinyl-2-pyrrolidinone (VP) and
poly(ethyleneglycol) acrylate (PEG-A)
7
curcumin (CMN)-loaded nanostructure
hybrid lipid capsules (CMN-nHLCs) of
three sizes (25, 75, and 150 nm) with 4%
(w/w) loading capacity
8
solid lipid nanoparticles (SLNs) derived
from S-(−)-γ-amino-α-hydroxybutyric
acid (GAHBA), γ-aminobutyric acid
(GABA)
9
Diblock dendrosome nanopolymer
(OM200)
10
mannose surface-modified solid lipid
nanoparticles (SLNs)
11
curcumin-loaded poly(ε-caprolactone)-
poly(ethylene glycol)-poly-
caprolactone) (PCL-PEG-PCL, PCEC)
nanofibers
12
CUR-loaded polyvinyl pyrrolidone
(CUR@PVP)
CONCLUSIONS AND POSSIBLE FUTURE EXTENSION
Degradation in aqueous medium specifically in higher pH narrowed down the various biological applications of
curcumin. In this discussion we have demonstrated various work which can cross the barrier by forming stable
complex/conjugate with curcumin in biological medium. However, it is important to consider interaction of
curcumin with various proteins of human body and various spectroscopic data (fluorescence, UV-vis, CD) along
with computational data unraveled the pattern of interactions. Curcumin is hydrophobic molecule so it binds
with unfolded state of HSA at hydrophobic subdomains IIA, IB and IIIA. People also deliver curcumin in live
normal and cancer cells and in mice model via intravenous injection using phospholipid vehicle. Many of those
delivery agents are not only invasive, biocompatible but also the whole drug delivery system is non toxic towards
non cancer cell. Nanocurcumin is more active and efficient than curcumin so nanoparticles were used for delivery
of curcumin. Different types of cell lines differs in various properties so different types of delivery system is
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needed for optimazion of bioavailability inside live cell as well as tumor/tissues. Cancer cell specific delivery
system should be developed for maximization of concentration of curcumin inside cell and hence to increase
rate of cell death with minimum drug concentration. Proper drug delivery system is also effective for showing
antitumor activity for prolonged time which may help to carry out different experiments. Proper delivery system
may help to understand mechanism of cell death, various dynamical processes, interactions of curcumin with
different organelles of cell. Several works on dynamics of interaction of curcumin with biological important
molecules as well as biomolecules should be done in future. Moreover, study on dynamical interaction with
various locations (organelles) of live cell should also be done for better understanding. Beside these synergistic
effect of those systems should be studied for minimum side effects of those delivery systems. Available studies
on cell should be propagated to tissue, tumour or animal model for real applications. Clinical trial may be carried
out with those drug delivery vehicle- curcumin conjugate systems.
Conflicts of interest
There are no conflicts of interests to declare.
REFERENCES
1. A Goel, A. B. Kunnumakkara, B. B. Aggarwal. “Curcumin as Curecumin”: from kitchen to clinic,”
Biochem. Pharmacol 75 (2008): 787−809.
2. G. Bar-Sela, R. Epelbaum, M. Schaffer, “Curcumin as an anti-cancer agent: review of the gap between
basic and clinical applications,” Curr Med Chem. 17 (2010): 190-197.
3. J. S. Jurenka, “Anti-inflammatory properties of curcumin, a major constituent of Curcuma longa: a
review of preclinical and clinical research,” Altern. Med. Rev.14 (2009): 141-153.
4. R. K. Maheshwari, A. K. Singh, J. Gaddipati, R. C. Srimal, “Multiple biological activities of curcumin:
a short review,” Life Sci. 78 (2006): 2081-2087.
5. A. S. Strimpakos, R. A. Sharma, “Curcumin: preventive and therapeutic properties in laboratory studies
and clinical trials,” Antioxid. Redox Signal 10 (2008): 511-545.
6. R. A. Sharma, W. P. Steward, A. J. Gescher, “Pharmacokinetics and pharmacodynamics of curcumin,”
Adv. Exp. Med. Biol. 595 (2007): 453-470.
7. A. Krishnamoorthy 1950. The wealth of India: a dictionary of indian raw materials and industrial
products. Vol. 2, p. 402. CSIR, New Delhi.
8. O. P. Sharma, “Antioxidant activity of curcumin and related compounds,” Biochem. Pharmacol. 25
(1976): 18111812.
9. N. Sreejayan, T. P. A. Devasagayam, K. I. Priyadarsini, M. N. A. Rao, “Inhibition of radiation induced
lipid peroxidation by curcumin,” Int. J. Pharmacol. 151 (1997): 127130.
10. K. I. Priyadarsini, “Free radical reaction of curcumin in membrane models,” Free Radic. Biol. Med. 23,
no. 6 (1997): 838843.
11. S. M. Khopde, K. I. Priyadarsini, P. Venkatesan, M. N. A. Rao, “Free radical scavenging ability and
antioxidant efficiency of curcumin and its substituted analogue,” Biophys. Chem. 80 (1999): 8591.
12. G. M. Cole, B. Teter, S. A. Frautschy,. “Curcumin as ″Curecumin″: from kitchen to clinic,” Adv. Exp.
Med. Biol. 595 (2007): 197− 212.
13. G. P. Lim, T. Chu, F. S. Yang, W. Beech, S. A. Frautschy, G. M. Cole, The curry spice curcumin reduces
oxidative damage and amyloid pathology in an Alzheimer transgenic mouse,” J. Neurosci. 21 (2001):
8370−8377.
14. FYang, G. P. Lim, A. N. Begum, O. J. Ubeda, M. R. Simmons, S. S. Ambegaokar, P. P. Chen, R. Kayed,
C. G. Glabe, S. A. Frautschy, G. M. Cole, “Curcumin inhibits formation of amyloid beta oligomers and
fibrils, binds plaques, and reduces amyloid in vivo,” J. Biol. Chem. 280 (2005): 5892−5901.
15. G. Khuwaja, M. M. Khan, T. Ishrat, A. Ahmad, S. S. Raza, M. Ashafaq, H. Javed, M. B. Khan, A. Khan,
K. Vaibhav, M. M. Safhi, F. Islam, “Neuroprotective effects of curcumin on 6- hydroxydopamine-
induced Parkinsonism in rats: behavioral, neuro- chemical and immunohistochemical studies,” Brain
Res. 1368 (2011): 254−263.
16. M. A. Hickey, C. Zhu, V. Medvedeva, R. P. Lerner, S. Patassini, N. R. Franich, P. Maiti, S. A. Frautschy,
S. Zeitlin, M. S. Levine, M. F. Chesselet, Improvement of neuropathology and transcriptional deficits
Page 505
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in CAG 140 knock-in mice supports a beneficial effect of dietary curcumin in Huntington’s disease,”
Mol. Neurodegener. 7 (2012): 12.
17. Y. J. Wang, M. H. Pan, A. L. Cheng, L. I. Lin, Y. S. Ho, C. Y. Hsieh, J. K. Lin, “Stability of curcumin
in buffer solutions and characterization of its degradation products,” J. Pharm. Biomed. Anal. 15 (1997):
1867-1876.
18. P. Anand, A. B. Kunnumakkara, R. A. Newman, B. B. Aggarwal,. “Bioavailability of curcumin:
problems and promises,” Mol. Pharm. 4 (2007): 807-818.
19. A. L. Cheng, C. H. Hsu, J. K. Lin, M. M. Hsu, Y. F. Ho, T. S. Shen, J. Y. Ko, J. T. Lin, B. R. Lin, W.
Ming-Shiang, H. S. Yu, S. H. Jee, G. S. Chen, T. M. Chen, C. A. Chen, M. K. Lai, Y. S. Pu, M. H. Pan,
Y. J. Wang, C. C. Tsai, C. Y. Hsieh, “Phase I clinical trial of curcumin, a chemopreventive agent, in
patients with high-risk or pre-malignant lesions,” Anticancer Res. 21 (2001): 28952900.
20. N. Dhillon, B. B. Aggarwal, R. A. Newman, R. A. Wolff, A. B. Kunnumakkara, J. L. Abbruzzese, C. S.
Ng, V. Badmaev, R. Kurzrock, Phase II trial of curcumin in patients with advanced pancreatic cancer,”
Clin. Cancer Res. 14 (2008): 44914499.
21. K. I. Priyadarsini, Photophysics, photochemistry and photobiology of curcumin: Studies from organic
solutions, bio-mimetics and living cells,” J. Photochem. and Photobio. C: Photochem. Rev. 10 (2009):
85-91.
22. M. Ghosh, N. Sarkar, “Exploring the World of Curcumin: Photophysics, Photochemistry, and
Applications in Nanoscience and Biology,” ChemBioChem. 25, no. 23 (2024): e202400335.
23. N. Bera, S. Layek, S. Pramanik, P. K. Nandi, R. Hazra, N. Sarkar, Ultrafast Dynamics of the Medicinal
Pigment Curcumin inside the Imidazolium Surface Active Ionic Liquid Containing Giant Vesicles and
White Light Generation via Triple-FRET Technique,” Langmuir 39 (2023): 11653−11663.
24. Mandal S, Banerjee C, Ghosh S, Kuchlyan J, Sarkar N. 2013. Modulation of the Photophysical Properties
of Curcumin in Nonionic Surfactant (Tween-20) Forming Micelles and Niosomes: A Comparative Study
of Different Microenvironments. J. Phys. Chem. B. 117 (23): 69576968
25. M. M. Yallapua, M. Jaggi, S. C. Chauhana, “β-Cyclodextrin-curcumin self-assembly enhances curcumin
delivery in prostate cancer cells, Colloids Surf. B: Biointerfaces 79 (2010): 113125.
26. Harada T, Pham D, Leung M. H. M, Ngo H. T, Lincoln S. F, Easton C. J, Kee T. W. 2011. Cooperative
Binding and Stabilization of the Medicinal Pigment Curcumin by Diamide Linked γ-Cyclodextrin
Dimers: A Spectroscopic Characterization. J. Phys. Chem. B. 115: 12681274.
27. T. Harada, H. L. Mc Ternan, D. Pham, S. F. Lincoln, T. W. Kee “Femtosecond Transient Absorption
Spectroscopy of the Medicinal Agent Curcumin in Diamide Linked γ‑Cyclodextrin Dimers,” J. Phys.
Chem. B 119 (2015): 2425−2433.
28. A. Gupta,
S. M. Briffa, S. Swingler, H. Gibson, V. Kannappan, G. Adamus, M. Kowalczuk, C. Martin,
I. Radecka, Synthesis of Silver Nanoparticles Using Curcumin-Cyclodextrins Loaded into Bacterial
Cellulose-Based Hydrogels for Wound Dressing Applications,” Biomacromolecules 21 (2020):
1802−1811.
29. F. Zsila, Z. Bikádi, M. Simonyi, “Unique, pH-dependent biphasic band shape of the visible circular
dichroism of curcuminserum albumin complex,” Biochem. Biophys. Res. Commun. 301 (2003): 776
782.
30. F. Zsila, Z. Bika ´di, M. Simonyi, “Molecular basis of the Cotton effects induced by the binding of
curcumin to human serum albumin,” Tetrahedron Asym. 14 (2003): 24332444.
31. M. Maciazek-Jurczyk, M. Maliszewska, J. Pozycka, J. Równicka-Zubik, A. ra, A. Sułkowska,
Tamoxifen and curcumin binding to serum albumin. Spectroscopic study J. Mol. Struct. 1044 (2013):
194200.
32. D. Patra, C. Barakat, R. M. Tafech, “Study on effect of lipophilic curcumin on sub-domain IIA site of
human serum albumin during unfolded and refolded states: A synchronous fluorescence spectroscopic
study,” Colloids Surf. B: Biointerfaces 94 (2012): 354 361.
33. M. H. M. Leung, T. W. Kee, “Effective Stabilization of Curcumin by Association to Plasma Proteins:
Human Serum Albumin and Fibrinogen,” Langmuir 25, no.10 (2009): 57735777.
34. P. K. Singh, V. Kotia, D. Ghosh, G. M. Mohite, A. Kumar, S. K. Maji, Curcumin Modulates α‑Synuclein
Aggregation and Toxicity,” ACS Chem. Neurosci. 4 (2013): 393−407.
Page 506
www.rsisinternational.org
INTERNATIONAL JOURNAL OF LATEST TECHNOLOGY IN ENGINEERING,
MANAGEMENT & APPLIED SCIENCE (IJLTEMAS)
ISSN 2278-2540 | DOI: 10.51583/IJLTEMAS | Volume XV, Issue IV, April 2026
35. A. Kunwar, A. Barik, R. Pandey, K. I. Priyadarsini, “Transport of liposomal and albumin loaded
curcumin to living cells: An absorption and fluorescence spectroscopic study,” Biochim. Biophys. Acta.
1760 (2006): 1513 1520.
36. M. Fatemizadeh, F. Tafvizi, F. Shamsi, S. Amiri, A. Farajzadeh, I. Akbarzadeh, “Apoptosis Induction,
Cell Cycle Arrest and Anti-Cancer Potential of Tamoxifen-Curcumin Loaded Niosomes Against MCF-
7 Cancer Cells,” Iran J. Pathol. 17, no.2 (2022): 183- 190.
37. T. Harada, L. Giorgio, T. J. Harris, D. Pham, H. T. Ngo, E. F. Need, B. J. Coventry, S. F. Lincoln, C. J.
Easton, G. Buchanan, T. W. Kee, “Diamide Linked γ‑Cyclodextrin Dimers as Molecular-Scale Delivery
Systems for the Medicinal Pigment Curcumin to Prostate Cancer Cells,” Mol. Pharmaceutics. 10 (2013):
4481−4490.
38. A. Kunwar, A. Barik, B. Mishra, K. Rathinasamy, R. Pandey, K. I. Priyadarsini, “Quantitative cellular
uptake, localization and cytotoxicity of curcumin in normal and tumor cells,” Biochim. Biophys. Acta.
1780 (2008): 673 679.
39. A. Safavy, K. P. Raisch, S. Mantena, L. L. Sanford, S. W. Sham, N. R. Krishna, J. A. Bonner, “Design
and Development of Water-Soluble Curcumin Conjugates as Potential Anticancer Agents,” J. Med.
Chem. 50 (2007): 6284 - 6288.
40. K. Sou, S. Inenaga, S. Takeoka, E. Tsuchida “Loading of curcumin into macrophages using lipid-based
nanoparticles,” Int. J. Pharm. 352 (2008): 287293
41. B. Lu, Y. Zhong, J. Zhang,. “Curcumin-Based Ionic Liquid Hydrogel for Topical Transdermal Delivery
of Curcumin To Improve Its Therapeutic Effect on the Psoriasis Mouse Model,” ACS Appl. Mater.
Interfaces 16, no. 14 (2024): 17080 17091.
42. I. A. Bhat,
R. Jain, M. M. Siddiqui, D. K. Saini, P. S. Mukherjee, “Water-Soluble Pd
8
L
4
Self-assembled
Molecular Barrel as an Aqueous Carrier for Hydrophobic Curcumin,” Inorg. Chem. 56 (2017):
5352−5360.
43. S. Bisht, G. Feldmann, S. Soni, R. Ravi, C. Karikar, A. Maitra, “Polymeric nanoparticle-encapsulated
curcumin (“nanocurcumin"): a novel strategy for human cancer therapy,” J. Nanobiotechnol. 5 (2007):
3.
44. S. K. Yadava, S. M. Basu, R. Valsalakumari, M. Chauhan, M. Singhania, J. Giri, “Curcumin-Loaded
Nanostructure Hybrid Lipid Capsules for Co-eradication of Breast Cancer and Cancer Stem Cells with
Enhanced Anticancer Efficacy,” ACS Appl. Bio Mater. 3, no. 10 (2020): 68116822.
45. S. Patra, J. Dey,
A. Chakraborty, “Physicochemical Characterization, Stability, and In Vitro Evaluation
of Curcumin-Loaded Solid Lipid Nanoparticles Prepared Using Biocompatible Synthetic Lipids,” ACS
Appl. Bio Mater. 6 (2023): 2785−2794.
46. S. Hajigholami, Z. V. Malekshahi, N. Bodaghabadi, F. Najafi, H. Shirzad, M. Sadeghizadeh “Nano
Packaged Tamoxifen and Curcumin; Effective Formulation against Sensitive and Resistant MCF-7
Cells,” Iran. J. Pharm. Res. 17, no. 1 (2018): 1-10.
47. J. Chae, Y. Choi, J. Hong, N. Kim, J. Kim, H. Y. Lee, J. Choi “Anti cancer and Antibacterial Properties
of Curcumin-Loaded Mannosylated Solid Lipid Nanoparticles for the Treatment of Lung Disease,” ACS
Appl. Bio Mater. 7 (2024): 2175−2185.
48. D. H. Hanna, G. R. Saad, Nanocurcumin: preparation, characterization and cytotoxic effects towards
human laryngeal cancer cells,” RSC Adv. 10 (2020): 20724-20737.
49. G. Guo, S. Z. Fu, L. X. Zhou, H. Liang, M. Fan, F. Luo, Z. Y. Qian, Y. Q. Wei “Preparation of curcumin
loaded poly(ε-caprolactone)-poly(ethylene glycol)-poly-caprolactone) nanofibers and their in vitro
antitumor activity against Glioma 9L cells” Nanoscale 3 (2011): 3825-3832.
50. C. Wang, C. Ma, Z. Wu, H. Liang, P. Yan, J. Song, N. Ma, Q. Zhao “Enhanced Bioavailability and
Anticancer Effect of Curcumin-Loaded Electrospun Nanofiber: In Vitro and In Vivo Study Nanoscale
Res Lett. 10, no. 1 (2015): 439.