Investigation of the Interaction Between Novel Spiro Thiazolo[3,2-a][1,3,5]Triazines and Bovine Serum Albumin by Spectroscopic Methods

Yang, Ying; Yu, Xianyong; Tong, Wenhua; Lu, Shiyu; Liu, Heting; Yao, Qin; Zhou, Hu

doi:10.1007/s10953-013-9975-z

Cited by 6 publications

(2 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…BSA is a large globular protein with 583 amino acid residues and consists of three homologous domains (I-III) which are divided into 9 loops connected by 17 disulfide bonds. 9 BSA has two tryptophan residues (Trp-134 and Trp-212) that possess intrinsic fluorescence. The former is located on the hydrophilic surface of the protein in subdomain IB, whereas the latter is buried in a hydrophobic pocket of subdomain IIA, which corresponds to the so-called Sudlow I binding site.…”

Section: Introductionmentioning

confidence: 99%

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

Peng

Wang

et al. 2015

Food Funct.

View full text Add to dashboard Cite

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

show abstract

Section: Introductionmentioning

confidence: 99%