Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

Leung, Mandy H. M.; Kee, Tak W.

doi:10.1021/la804215v

Cited by 184 publications

(176 citation statements)

References 36 publications

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“…However, for Cur NPs, there were no obvious reductions to be observed under the same conditions. Similar results have been reported by Leung and Kee (2009), where the authors claimed that under the neutral pH condition Cur could degrade by about 90 % within 30 min at room temperature. In ambient conditions, the Cur NPs in CPH and NaCas were still very stable in 6 h storage compared with the free Cur in PBS (Fig.…”

Section: The Chemical Stability Of Cur Npssupporting

confidence: 89%

Comparison of the colloidal stability, bioaccessibility and antioxidant activity of corn protein hydrolysate and sodium caseinate stabilized curcumin nanoparticles

et al. 2016

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The aims of this work were to construct corn protein hydrolysate (CPH)-based curcumin nanoparticles (Cur NPs) and to compare the colloidal stability, bioaccessibility and antioxidant activity of the Cur NPs stabilized CPH and sodium caseinate (NaCas) respectively. The results indicated that Cur solubility could be considerably improved after the Cur NPs fabrication. The spectroscopy results demonstrated that the solubilization of Cur should be attributed to its complexation with CPH or NaCas. The Cur NPs exhibited good colloidal stability after 1 week's storage but showed smaller (40 nm) size in CPH than in NaCas (100 nm). After lyophilization, the Cur NPs powders showed good rehydration properties and chemical stability, and compared with NaCas, the size of Cur NPs stabilized by CPH was still smaller. Additionally, the Cur NPs exhibited higher chemical stability against the temperature compared with free Cur, and the CPH could protect Cur from degradation more efficiently. Comparing with NaCas, the Cur NPs stabilized by CPH exhibited better bioaccessibility and antioxidant activity. This study demonstrated that CPH may be better than NaCas in Cur NPs fabrication and it opens up the possibility of using hydrophobic protein hydrolysate to construct the NPs delivery system.

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Section: The Chemical Stability Of Cur Npssupporting

confidence: 89%

Comparison of the colloidal stability, bioaccessibility and antioxidant activity of corn protein hydrolysate and sodium caseinate stabilized curcumin nanoparticles

et al. 2016

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“…It has been reported that the stability of curcumin increases when bound to plasma proteins or loaded in nanoformulations (39)(40)(41). We therefore studied the degradation of curcumin in two different formulations, namely loaded in mPEG-HPMA-Bz micelles and in Triton X-100 micelles.…”

Section: Degradation Of Curcumin (As Curcuminoid Mixture) Loaded In Mmentioning

confidence: 99%

A Kinetic Degradation Study of Curcumin in Its Free Form and Loaded in Polymeric Micelles

Naksuriya

Steenbergen

Toraño

et al. 2016

AAPS J

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Abstract. Curcumin, a phenolic compound, possesses many pharmacological activities and is under clinical evaluation to treat different diseases. However, conflicting data about its stability have been reported. In this study, the kinetic degradation of curcumin from a natural curcuminoid mixture under various conditions (pH, temperature, and dielectric constant of the medium) was investigated. Moreover, the degradation of pure curcumin at some selected conditions was also determined. To fully solubilize curcumin and to prevent precipitation of curcumin that occurs when low concentrations of co-solvent are present, a 50:50 (v/v) aqueous buffer/methanol mixture was used as standard medium to study its degradation kinetics. The results showed that degradation of curcumin both as pure compound and present in the curcuminoid mixture followed first order kinetic reaction. It was further shown that an increasing pH, temperature, and dielectric constant of the medium resulted in an increase in the degradation rate. Curcumin showed rapid degradation due to autoxidation in aqueous buffer pH=8.0 with a rate constant of 280×10 -3 h -1, corresponding with a half-life (t 1/2 ) of 2.5 h. Dioxygenated bicyclopentadione was identified as the final degradation product. Importantly, curcumin loaded as curcuminoid mixture in ω-methoxy poly (ethylene glycol)-b-(N-(2-benzoyloxypropyl) methacrylamide) (mPEG-HPMA-Bz) polymeric micelles and in Triton X-100 micelles was about 300-500 times more stable than in aqueous buffer. Therefore, loading of curcumin into polymeric micelles is a promising approach to stabilize this compound and develop formulations suitable for further pharmaceutical and clinical studies.

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“…Because of the low aqueous solubility, curcumin tends to aggregate and precipitate in water, limiting its bioavailability. [13][14][15][16] In addition, curcumin undergoes rapid degradation in water and buffer solutions, with a reaction half-life of 9.5 min at pH 7.2. 17 It has been demonstrated that the degradation is mostly due to deprotonation of curcumin, producing the degradation products vanilin, ferulic acid, and feruroyl methane.…”

Section: Introductionmentioning

confidence: 99%

Excited-State Intramolecular Hydrogen Atom Transfer of Curcumin in Surfactant Micelles

et al. 2010

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Femtosecond fluorescence upconversion experiments were performed on the naturally occurring medicinal pigment, curcumin, in anionic, cationic, and neutral micelles. In our studies, the micelles are composed of sodium dodecyl sulfate (SDS), dodecyl trimethyl ammonium bromide (DTAB), and triton X-100 (TX-100). We demonstrate that the excited-state kinetics of curcumin in micelles have a fast (3−8 ps) and slow (50−80 ps) component. While deuteration of curcumin has a negligible effect on the fast component, the slow component exhibits a pronounced isotope effect of ∼1.6, indicating that micelle-captured curcumin undergoes excited-state intramolecular hydrogen atom transfer. Studies of solvation dynamics of curcumin in a 10 ps time window reveal a fast component (≤300 fs) followed by a 8, 6, and 3 ps component in the solvation correlation function for the TX-100, DTAB, and SDS micelles, respectively. October 23, 2009; ReVised Manuscript ReceiVed: January 4, 2010 Femtosecond fluorescence upconversion experiments were performed on the naturally occurring medicinal pigment, curcumin, in anionic, cationic, and neutral micelles. In our studies, the micelles are composed of sodium dodecyl sulfate (SDS), dodecyl trimethyl ammonium bromide (DTAB), and triton X-100 (TX-100). We demonstrate that the excited-state kinetics of curcumin in micelles have a fast (3-8 ps) and slow (50-80 ps) component. While deuteration of curcumin has a negligible effect on the fast component, the slow component exhibits a pronounced isotope effect of ∼1.6, indicating that micelle-captured curcumin undergoes excited-state intramolecular hydrogen atom transfer. Studies of solvation dynamics of curcumin in a 10 ps time window reveal a fast component (e300 fs) followed by a 8, 6, and 3 ps component in the solvation correlation function for the TX-100, DTAB, and SDS micelles, respectively. Keywords

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Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

Cited by 184 publications

References 36 publications

Comparison of the colloidal stability, bioaccessibility and antioxidant activity of corn protein hydrolysate and sodium caseinate stabilized curcumin nanoparticles

Comparison of the colloidal stability, bioaccessibility and antioxidant activity of corn protein hydrolysate and sodium caseinate stabilized curcumin nanoparticles

A Kinetic Degradation Study of Curcumin in Its Free Form and Loaded in Polymeric Micelles

Excited-State Intramolecular Hydrogen Atom Transfer of Curcumin in Surfactant Micelles

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