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.
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]
Structural basis of a temporin 1b analogue antimicrobial activity against gram negative bacteria determined by CD and NMR techniques in cellular environment
A. Romanelli
;
2015
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.
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