Please use this identifier to cite or link to this item: http://hdl.handle.net/10316/18082
Title: FTIR spectroscopy structural analysis of the interaction between Lactobacillus kefir S-layers and metal ions
Authors: Gerbino, E. 
Mobili, P. 
Tymczyszyn, E. 
Fausto, R. 
Gómez-Zavaglia, A. 
Issue Date: Feb-2011
Publisher: Elsevier
Serial title, monograph or event: Journal of Molecular Structure
Volume: 987
Abstract: FTIR spectroscopy was used to structurally characterize the interaction of S-layer proteins extracted from two strains of Lactobacillus kefir (the aggregating CIDCA 8348 and the non-aggregating JCM 5818) with metal ions (Cd+2, Zn+2, Pb+2 and Ni+2). The infrared spectra indicate that the metal/protein interaction occurs mainly through the carboxylate groups of the side chains of Asp and Glut residues, with some contribution of the NH groups belonging to the peptide backbone. The frequency separation between the νCOO− anti-symmetric and symmetric stretching vibrations in the spectra of the S-layers in presence of the metal ions was found to be ca. 190 cm−1 for S-layer CIDCA 8348 and ca. 170 cm−1 for JCM 5818, denoting an unidentate coordination in both cases. Changes in the secondary structures of the S-layers induced by the interaction with the metal ions were also noticed: a general trend to increase the amount of β-sheet structures and to reduce the amount of α-helices was observed. These changes allow the proteins to adjust their structure to the presence of the metal ions at minimum energy expense, and accordingly, these adjustments were found to be more important for the bigger ions.
URI: http://hdl.handle.net/10316/18082
DOI: 10.1016/j.molstruc.2010.12.012
Rights: openAccess
Appears in Collections:FCTUC Química - Artigos em Revistas Internacionais

Files in This Item:
File Description SizeFormat
Journal of Molecular Structure, 987 (2011) 186.pdf741.15 kBAdobe PDFView/Open
Show full item record

SCOPUSTM   
Citations

33
checked on Jun 25, 2019

WEB OF SCIENCETM
Citations

33
checked on Jun 25, 2019

Page view(s)

184
checked on Oct 14, 2019

Download(s)

102
checked on Oct 14, 2019

Google ScholarTM

Check

Altmetric

Dimensions


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