Investigation of the interaction between patulin and human serum albumin by a spectroscopic method, atomic force microscopy, and molecular modeling.

ABSTRACT: The interaction of patulin with human serum albumin (HSA) was studied in vitro under normal physiological conditions. The study was performed using fluorescence, ultraviolet-visible spectroscopy (UV-Vis), circular dichroism (CD), atomic force microscopy (AFM), and molecular modeling techniques. The quenching mechanism was investigated using the association constants, the number of binding sites, and basic thermodynamic parameters. A dynamic quenching mechanism occurred between HSA and patulin, and the binding constants (K) were 2.60 × 10(4), 4.59 × 10(4), and 7.01 × 10(4) M(-1) at 288, 300, and 310 K, respectively. Based on fluorescence resonance energy transfer, the distance between the HSA and patulin was determined to be 2.847 nm. The ΔG (0), ΔH (0), and ΔS (0) values across various tem

SUBMITTER: Yuqin L 

PROVIDER: S-EPMC4119689 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature