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The mechanism of action of antimicrobial peptides: lipid vesicles vs. bacteria
Melo, Manuel N.; Castanho, Miguel A. R. B.Copyright © 2012 Melo and Castanho. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
Using zeta-potential measurements to quantify peptide partition to lipid membranes
Freire, João M.; Domingues, Marco M.; Matos, Joana; Melo, Manuel N.; Veiga, Ana Salomé; Santos, Nuno C.; Castanho, Miguel A. R. B.© The Author(s) 2011. This article is published with open access at Springerlink.com. ; Open Access: This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. ; Many cellular phenomena occur on the biomembranes. There are plenty...
Quantifying molecular partition of charged molecules by Zeta-potential measurem...
Freire, João Miguel; Domingues, Marco M.; Matos, Joana; Melo, Manuel N.; Veiga, Ana Salomé; Santos, Nuno C.; Castanho, Miguel A. R. B.Copyright ©2010 The European Peptide Society
Synergistic effects of the membrane actions of cecropin-melittin antimicrobial ...
Ferre, Rafael; Melo, Manuel N.; Correia, Ana D.; Feliu, Lidia; Bardají, Eduard; Planas, Marta; Castanho, Miguel© 2009 by the Biophysical Society ; BP100 (KKLFKKILKYL-NH2) is a short cecropin A-melittin hybrid peptide, obtained through a combinatorial chemistry approach, which is highly effective in inhibiting both the in vitro and in vivo growth of economically important plant pathogenic Gram-negatives. The intrinsic Tyr fluorescence of BP100 was taken advantage of to study the peptide’s binding affinity and damaging e...
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