Unknown

Dataset Information

0

Diverse Effects of Different "Protein-Based" Vehicles on the Stability and Bioavailability of Curcumin: Spectroscopic Evaluation of the Antioxidant Activity and Cytotoxicity In Vitro.


ABSTRACT:

Background

Curcumin is a natural polyphenolic compound with anti-cancer, antiinflammatory, and anti-oxidation properties. Low water solubility and rapid hydrolytic degradation are two challenges limiting use of curcumin.

Objective

In this study, the roles of the native/modified forms of Bovine Serum Albumin (BSA), ?-lactoglobulin (?-lg) and casein, as food-grade biopolymers and also protein chemical modification, in stabilizing and on biological activity of curcumin were surveyed.

Methods

In this article, we used various spectroscopic as well as cell culture-based techniques along with calculation of thermodynamic parameters.

Results

Investigation of curcumin stability indicated that curcumin binding to the native BSA and modified ? -lg were stronger than those of the modified BSA and native ? -lg, respectively and hence, the native BSA and modified ?-lg could suppress water-mediated and light-mediated curcumin degradation, significantly. Moreover, in the presence of the native proteins (BSA and casein), curcumin revealed elevated in vitro anti-cancer activity against MCF-7 (human breast carcinoma cell line) and SKNMC (human neuroblastoma cell line). As well, curcumin, in the presence of the unmodified "BSA and ?-lg", was more potent to decrease ROS generation by hydrogen peroxide (H2O2) whereas it led to an inverse outcome in the presence of native casein. Overall, in the presence of the protein-bound curcumin, increased anti-cancer activity and decreased ROS generation by H2O2 in vitro were documented.

Conclusion

It appears that "water exclusion" is major determinant factor for increased stability/ efficacy of the bound curcumin so that some protein-curcumin systems may provide novel tools to increase both food quality and the bioavailability of curcumin as health promoting agent.

SUBMITTER: Mirzaee F 

PROVIDER: S-EPMC6416488 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

altmetric image

Publications

Diverse Effects of Different "Protein-Based" Vehicles on the Stability and Bioavailability of Curcumin: Spectroscopic Evaluation of the Antioxidant Activity and Cytotoxicity In Vitro.

Mirzaee Farideh F   Hosseinzadeh Leila L   Ashrafi-Kooshk Mohammad Reza MR   Esmaeili Sajjad S   Ghobadi Sirous S   Farzaei Mohammad Hosein MH   Zad-Bari Mahmoud Reza MR   Khodarahmi Reza R  

Protein and peptide letters 20190101 2


<h4>Background</h4>Curcumin is a natural polyphenolic compound with anti-cancer, antiinflammatory, and anti-oxidation properties. Low water solubility and rapid hydrolytic degradation are two challenges limiting use of curcumin.<h4>Objective</h4>In this study, the roles of the native/modified forms of Bovine Serum Albumin (BSA), β-lactoglobulin (β-lg) and casein, as food-grade biopolymers and also protein chemical modification, in stabilizing and on biological activity of curcumin were surveyed.  ...[more]

Similar Datasets

| S-EPMC6384587 | biostudies-literature
| S-EPMC8347926 | biostudies-literature
| S-EPMC7593682 | biostudies-literature
| S-EPMC6407602 | biostudies-literature
| S-EPMC6106897 | biostudies-other
| S-EPMC6268932 | biostudies-literature
| S-EPMC5946112 | biostudies-literature
| S-EPMC8957331 | biostudies-literature
| S-EPMC4943321 | biostudies-literature
| S-EPMC8708738 | biostudies-literature