TY - JOUR
T1 - Antimicrobial Activity and Bacterial-Membrane Interaction of Ovine-Derived Cathelicidins
AU - Anderson, Rachel C.
AU - Hancock, Robert E.W.
AU - Yu, Pak Lam
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2004/2
Y1 - 2004/2
N2 - Three ovine-derived cathelicidins, SMAP29, OaBac5mini, and OaBac7.5mini, were compared with respect to their antibacterial activities and interactions with membranes. SMAP29 was confirmed to be α-helical, broad spectrum, and able to disrupt both the outer and the cytoplasmic membranes at relatively low concentrations. In contrast, the two proline- and arginine-rich OaBac peptides had more-modest antibacterial activities, reduced levels of lipopolysaccharide binding, and a lesser ability to depolarize the cytoplasmic membrane, consistent with a cytoplasmic target.
AB - Three ovine-derived cathelicidins, SMAP29, OaBac5mini, and OaBac7.5mini, were compared with respect to their antibacterial activities and interactions with membranes. SMAP29 was confirmed to be α-helical, broad spectrum, and able to disrupt both the outer and the cytoplasmic membranes at relatively low concentrations. In contrast, the two proline- and arginine-rich OaBac peptides had more-modest antibacterial activities, reduced levels of lipopolysaccharide binding, and a lesser ability to depolarize the cytoplasmic membrane, consistent with a cytoplasmic target.
UR - http://www.scopus.com/inward/record.url?scp=0942301292&partnerID=8YFLogxK
U2 - 10.1128/AAC.48.2.673-676.2004
DO - 10.1128/AAC.48.2.673-676.2004
M3 - Article
C2 - 14742236
AN - SCOPUS:0942301292
VL - 48
SP - 673
EP - 676
JO - Antimicrobial Agents and Chemotherapy
JF - Antimicrobial Agents and Chemotherapy
SN - 0066-4804
IS - 2
ER -