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Enhanced amphiphilic profile of a short ß-stranded peptide improves its antimicrobial activity

Manzo, G.; Scorciapino, M.A.; Wadhwani, P.; Bürck, J.; Montaldo, N.P.; Pintus, M.; Sanna, R.; Casu, M.; Giuliani, A.; Pirri, G.; Luca, V.; Ulrich, A.S.; Rinaldi, A.C.

Abstract:
SB056 is a novel semi-synthetic antimicrobial peptide with a dimeric dendrimer scaffold. Active against both Gram-negative and -positive bacteria, its mechanism has been attributed to a disruption of bacterial membranes. The branched peptide was shown to assume a β- stranded conformation in a lipidic environment. Here, we report on a rational modification of the original, empirically derived linear peptide sequence [WKKIRVRLSA-NH$_{2}$, SB056-lin]. We interchanged the first two residues [KWKIRVRLSA-NH$_{2}$, β-SB056-lin] to enhance the amphipathic profile, in the hope that a more regular β-strand would lead to a better antimicrobial performance. MIC values confirmed that an enhanced amphiphilic profile indeed significantly increases activity against both Gram-positive and -negative strains. The membrane binding affinity of both peptides, measured by tryptophan fluorescence, increased with an increasing ratio of negatively charged/zwitterionic lipids. Remarkably, β- SB056-lin showed considerable binding even to purely zwitterionic membranes, unlike the original sequence, indicating that besides electrostatic attraction also the amphi ... mehr


Zugehörige Institution(en) am KIT Institut für Biologische Grenzflächen (IBG)
Publikationstyp Zeitschriftenaufsatz
Jahr 2015
Sprache Englisch
Identifikator ISSN: 1932-6203
URN: urn:nbn:de:swb:90-AAA1101010113
KITopen ID: 110101011
HGF-Programm 47.02.02; LK 01
Erschienen in PLoS one
Band 10
Seiten 1-18
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