albumin - publications

Predict more albumin - ligand interactions now!

1. Chirality. 2012 Apr 28. doi: 10.1002/chir.22024. [Epub ahead of print]

Chiral Recognition of Metalaxyl Enantiomers by Human Serum Albumin: Evidence from
Molecular Modeling and Photophysical Approach.

Ding F, Li XN, Diao JX, Sun Y, Zhang L, Sun Y.

Department of Chemistry, China Agricultural University, Beijing, China.

Metalaxyl is an acylamine fungicide, belonging to the most widely known member of
the amide group. This task is aimed to scrutinize binding region and spatial
structural change of principal vector human serum albumin (HSA) complex with
(R)-/(S)-metalaxyl by exploiting molecular modeling, steady-state and
time-resolved fluorescence, and circular dichroism (CD) approaches. According to
molecular modeling, (R)-metalaxyl is situated within subdomains IIA and IIIA and
the affinity of site I with (R)-metalaxyl is greater than site II, whereas
(S)-metalaxyl is only located at subdomain IIA and the affinity of (S)-metalaxyl
with site I is superior compared with that with (R)-metalaxyl. This coincides
with the competitive ligand binding, guanidine hydrochloride-induced unfolding of
protein, and hydrophobic 8-anilino-1-naphthalenesulfonic acid experiments; the
acting forces between (R)-/(S)-metalaxyl and HSA are hydrophobic, π-π
interactions, and hydrogen bonds, as derived from molecular modeling.
Fluorescence emission manifested that the complex of (R)-/(S)-metalaxyl to HSA is
the formation of adduct with an affinity of 10(4)  M(-1) , which corroborates the
time-resolved fluorescence that the static type was operated. Furthermore, the
changes of far-UV CD spectra evidence the polypeptide chain of HSA partially
unfolded after conjugation with (R)-/(S)-metalaxyl. Through this work, we
envisage that it can offer central clues on the biodistribution, absorption, and
bioaccumulation of (R)-/(S)-metalaxyl. © 2012 Wiley Periodicals, Inc.

Copyright © 2012 Wiley Periodicals, Inc.

PMID: 22544615 [PubMed - as supplied by publisher]