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 / Malgieri, Gaetano; Avitabile, Concetta; Palmieri, Maddalena; D'Andrea, LUCA DOMENICO; Isernia, Carla; Romanelli, Alessandra; Fattorusso, Roberto. - In: ACS CHEMICAL BIOLOGY. - ISSN 1554-8929. - 10:4(2015), pp. 965-9-969. [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
AVITABILE, CONCETTA;D'ANDREA, LUCA DOMENICO;ROMANELLI, ALESSANDRA;
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
