Structural differences among various dietary polyphenols affect their absorption, metabolism, and bioactivities. In this work, chlorogenic acid (CA) and its two positional isomers, neochlorogenic acid (NCA) and cryptochlorogenic acid (CCA), were investigated for their binding reactions with human serum albumin (HSA) using fluorescence, ultraviolet–visible, Fourier transform infrared and circular dichroism spectroscopies, as well as molecular docking. All three isomers were bound to HSA at Sudlow’s site I and affected the protein secondary structure. CCA presented the strongest ability of hydrogen-bond formation, and both CA and NCA generated more electrostatic interactions with HSA. The albumin-binding capacity of these compounds decreased in the order CCA > NCA > CA. The compound with 4-esteryl structure showed higher binding affinity and larger conformational changes to HSA than that with 3- or 5-esteryl structures. These comparative studies on structure–affinity relationship contributed to the structural modification and design of phenolic food additives or new polyphenol-like drugs.
... Different protein-ligand interactions were determined using a fresh albumin stock solution prepared on the same day. CA, NCA, and CCA (>99% by HPLC) were purchased from Biopurify Phytochemicals Ltd. (Chengdu, China). ...
Multispectroscopic and docking studies on the binding of chlorogenic acid isomers to human serum albumin: Effects of esteryl position on affinity
期刊名：Food Chemistry
文献编号：
文献地址： http://www.sciencedirect.com/science/article/pii/S0308814616309001
发表日期：1 December 2016
文献编号：
文献地址： http://www.sciencedirect.com/science/article/pii/S0308814616309001
发表日期：1 December 2016
