albumin - publications

Predict more albumin - ligand interactions now!


1. Spectrochim Acta A Mol Biomol Spectrosc. 2012 Mar 29;94C:23-29. [Epub ahead of
print]

Study on the interaction between novel spiro pyrrolidine and bovine serum albumin
by spectroscopic techniques.

Yu X, Yang Y, Zou X, Tao H, Ling Y, Yao Q, Zhou H, Yi P.

Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of
Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of
Chemistry and Chemical Engineering, Hunan University of Science and Technology,
Xiangtan 411201, China.

Spiro pyrrolidines, which were proved with diverse and potent biological
activities and they were discovered widespread in nature. In this paper, using
fluorescence and ultraviolet spectroscopy, we investigated the interactions
between novel spiro pyrrolidine (NSP) and bovine serum albumin (BSA) under the
imitated physiological condition. The results show that the NSP binds to BSA
molecules. Static quenching and non-radiation energy transfer are the main
reasons for fluorescence quenching. We calculated the binding constant (K(a)) and
binding sites (n) at different temperatures and obtained the binding distance
between the tryptophan residue in BSA and the NSP based on the Förster theory of
non-radiation energy transfer. In addition, using synchronous fluorescence
spectra, we demonstrated conformation changes of BSA caused by NSP. The
comparison of binding potency of NSP and BSA suggests that the substituent on the
benzene ring influences the binding ability of NSP and BSA.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22503872 [PubMed - as supplied by publisher]