Structural basis of a temporin 1b analogue antimicrobial activity against gram negative bacteria determined by CD and NMR techniques in cellular environment
Articolo
Data di Pubblicazione:
2015
Citazione:
Structural basis of a temporin 1b analogue antimicrobial activity against gram negative bacteria determined by CD and NMR techniques in cellular environment / M. Gaetano, A. Concetta, P. Maddalena, D. Luca Domenico, I. Carla, A. Romanelli, F. Roberto. - In: ACS CHEMICAL BIOLOGY. - ISSN 1554-8929. - 10:4(2015 Apr), pp. 965-969. [10.1021/cb501057d]
Abstract:
We here report an original approach to elucidate mechanisms of action of antimicrobial peptides and derive crucial structural requirements for the design of novel therapeutic agents. The high resolution structure of TB-KKG6A, an antimicrobial peptide designed to amplify the spectrum of action of Temporin B, bound to E. coli is here determined by means of CD and NMR methodologies. We have also defined, through STD analysis, the residues in closer proximity to the bacterial membrane.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
antimicrobial cationic peptides; cell membrane; circular dichroism; drug design; Escherichia coli; gram-negative bacteria; magnetic resonance spectroscopy;
Elenco autori:
M. Gaetano, A. Concetta, P. Maddalena, D. Luca Domenico, I. Carla, A. Romanelli, F. Roberto
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