Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6007
Title: A structurally driven analysis of thiol reactivity in mammalian albumins
Authors: Spiga, Ottavia 
Summa, D
Cirri, S
Bernini, A
Venditti, V
De Chiara, M
Priora, R
Frosali, S
Margaritis, A
Di, Giuseppe
Di Simplicio, P
Niccolai, Neri 
Issue Date: 2011
Project: None 
Journal: BIOPOLYMERS
Abstract: 
Understanding the structural basis of protein redox activity is still an open question. Hence, by using a structural genomics approach, different albumins have been chosen to correlate protein structural features with the corresponding reaction rates of thiol exchange between albumin and disulfide DTNB. Predicted structures of rat, porcine, and bovine albumins have been compared with the experimentally derived human albumin. High structural similarity among these four albumins can be observed, in spite of their markedly different reactivity with DTNB. Sequence alignments offered preliminary hints on the contributions of sequence-specific local environments modulating albumin reactivity. Molecular dynamics simulations performed on experimental and predicted albumin structures reveal that thiolation rates are influenced by hydrogen bonding pattern and stability of the acceptor C34 sulphur atom with donor groups of nearby residues. Atom depth evolution of albumin C34 thiol groups has been monitored during Molecular Dynamic trajectories. The most reactive albumins appeared also the ones presenting the C34 sulphur atom on the protein surface with the highest accessibility. High C34 sulphur atom reactivity in rat and porcine albumins seems to be determined by the presence of additional positively charged amino acid residues favoring both the C34 S(-) form and the approach of DTNB. (C) 2010 Wiley Periodicals, Inc. Biopolymers 95: 278-285, 2011.
Description: 
27394
URI: http://hdl.handle.net/20.500.12779/6007
ISSN: 0006-3525
DOI: 10.1002/bip.21577
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.