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Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSⁿ, and Molecular Docking Approach.

ABSTRACT: Clarified the binding mechanism of drugs with plasma proteins could provide fresh insights into the drug development. Caffeoylquinic acids (CQAs) are a kind of phenolic acid compounds which has extensive biological effects. This study investigated the binding mechanism of three CQAs, including chlorogenic acid, neochlorogenic acid, and cryptochlorogenic acid, with bovine serum albumin (BSA) by using multi-spectroscopic techniques, including fluorescence, UV-Vis, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy, LC-MSⁿ, molecular docking and antioxidant activity assessment. In addition, the influences of PBS buffer, Tris-HCl buffer and water as solvents on the characteristics of CQAs and BSA interaction were also investigated. The results showed that in

SUBMITTER: Jiao Q

PROVIDER: S-EPMC6909939 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSⁿ, and Molecular Docking Approach.

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Dataset Information

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSn, and Molecular Docking Approach.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Study on the Interactions Between Caffeoylquinic Acids With Bovine Serum Albumin: Spectroscopy, Antioxidant Activity, LC-MSⁿ, and Molecular Docking Approach.