Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi1011578
Title: Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides
Authors: Leptihn, S.
Har, J.Y.
Wohland, T. 
Ding, J.L. 
Issue Date: 2-Nov-2010
Citation: Leptihn, S., Har, J.Y., Wohland, T., Ding, J.L. (2010-11-02). Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides. Biochemistry 49 (43) : 9161-9170. ScholarBank@NUS Repository. https://doi.org/10.1021/bi1011578
Abstract: Antimicrobial peptides are key elements of the innate immune system. Many of them interact with membranes of bacteria leading to perturbation of the lipid bilayer and eventually to inactivation of the pathogen. The emergence of multidrug-resistant bacteria has necessitated innovations of new and more powerful classes of antimicrobials. Here we present the in-depth study of an antimicrobial peptide, MIRIAM, derived from Sushi1 (S1), a well-characterized peptide from the horseshoe crab. MIRIAM interacts strongly with negatively charged lipids, forming an α-helical structure. MIRIAM was found to neutralize LPS and kill Gram-negative bacteria with high efficiency, while not releasing LPS. The promising therapeutic potential of MIRIAM is shown by hemolytic assays, which demonstrate that eukaryotic membranes are unaffected at bactericidal concentrations. Nanoparticle-conjugated MIRIAM used in single-molecule fluorescence and electron microscopy experiments showed that MIRIAM targets bacterial membranes to kill bacteria similarly to parental S1. Furthermore, fragments derived from MIRIAM and S1 provided insights on their molecular mechanisms of action, in particular, the relationships of functional motifs comprised by charge, hydrophobicity, and structure within each peptide. We conclude that the combination of charge, hydrophobicity, and length of the peptide is important. A close interaction of amino acids in a single molecule in a carefully balanced ensemble of sequence position and secondary structure is crucial. © 2010 American Chemical Society.
Source Title: Biochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/75825
ISSN: 00062960
DOI: 10.1021/bi1011578
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

16
checked on Jul 19, 2018

WEB OF SCIENCETM
Citations

16
checked on Jun 25, 2018

Page view(s)

48
checked on Jun 29, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.