Author(s):
Gerbino, E. 
; Mobili, P. ; Tymczyszyn, E. ; Fausto, R. ; Gómez-Zavaglia, A.
Date: 2011
Persistent ID: http://hdl.handle.net/10316/18082
Origin: Estudo Geral - Universidade de Coimbra
Document details
FTIR spectroscopy structural analysis of the interaction between Lactobacillus ...
Description
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.
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.
Document Type
Article
Language English
Language English
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