作者: Xin Peng , Xiangchao Wang , Wei Qi , Renliang Huang , Rongxin Su
DOI: 10.1039/C5FO00597C
关键词:
摘要: Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol from plants of the mint family with potent biological activities. Here, in vitro interaction RA bovine serum albumin (BSA) has been investigated using various biophysical approaches as well molecular modeling methods, to ascertain its binding mechanism conformational changes. The fluorescence results demonstrated that quenching BSA by was mainly result formation a ground state BSA-RA complex, had one high affinity site constant 4.18 × 10(4) mol L(-1) at 298 K. Analysis thermodynamic parameters revealed hydrophobic hydrogen bond interactions were dominant intermolecular force complex formation. primary (site I) identified marker competitive experiments. distance between tryptophan residue evaluated 3.12 nm based on Forster's theory non-radiation energy transfer. UV-vis absorption, synchronous fluorescence, three-dimensional 8-anilino-1-naphthalenesulfonic (ANS) circular dichroism (CD), Fourier transform infrared (FT-IR) spectra confirmed conformation structure altered presence RA. Moreover, nuclear magnetic spectroscopy showed aromatic groups took part reaction during complexation. In addition, picture atomic level examined docking dynamics studies. brief, can bind noncovalent bonds relatively stable way, these findings will be beneficial functional food research