Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi1011578
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dc.titleCorrelation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides
dc.contributor.authorLeptihn, S.
dc.contributor.authorHar, J.Y.
dc.contributor.authorWohland, T.
dc.contributor.authorDing, J.L.
dc.date.accessioned2014-06-23T05:35:07Z
dc.date.available2014-06-23T05:35:07Z
dc.date.issued2010-11-02
dc.identifier.citationLeptihn, 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
dc.identifier.issn00062960
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/75825
dc.description.abstractAntimicrobial 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/bi1011578
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1021/bi1011578
dc.description.sourcetitleBiochemistry
dc.description.volume49
dc.description.issue43
dc.description.page9161-9170
dc.description.codenBICHA
dc.identifier.isiut000283409100005
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