Antimicrobial peptide RP-1 structure and interactions with anionic versus zwitterionic micelles
نویسندگان
چکیده
منابع مشابه
Interactions of an anionic antimicrobial peptide with Staphylococcus aureus membranes.
The antimicrobial activity of the anionic peptide, AP1 (GEQGALAQFGEWL), was investigated. AP1 was found to kill Staphylococcus aureus with an MLC of 3mM and to induce maximal surface pressure changes of 3.8 mN m(-1) over 1200s in monolayers formed from lipid extract of S. aureus membranes. FTIR spectroscopy showed the peptide to be alpha-helical (100%) in the presence of vesicles formed from th...
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The respiratory tract contains numerous antimicrobial factors necessary for normal innate pulmonary defense. Although many of these molecules reside in airway surface liquid (ASL) simultaneously, little information exists concerning antagonistic, additive, or synergistic interactions. Since both cationic lysozyme and anionic antimicrobial peptides (AP) are found in high concentrations in ASL, t...
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Structure-mechanism relationships are key determinants of host defense peptide efficacy. These relationships are influenced by anatomic, physiologic and microbiologic contexts. Structure-mechanism correlates were assessed for the synthetic peptide RP-1, modeled on microbicidal domains of platelet kinocidins. Antimicrobial efficacies and mechanisms of action against susceptible ((S)) or resistan...
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In this work small angle X-ray scattering (SAXS) studies on the interaction of the phenothiazine trifluoperazine (TFP, 2-10 mM), a cationic drug, with micelles of the zwitterionic surfactant 3-(N-hexadecyl-N,N-dimethylammonium) propane sulfonate (HPS, 30 mM) and the anionic surfactant sodium dodecyl sulfate (SDS, 40 mM) at pH 4.0, 7.0, and 9.0 are reported. The data were analyzed through the mo...
متن کاملStructure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold.
Tritrpticin is a member of the cathelicidin family, a group of diverse antimicrobial peptides found in neutrophil granules. The three Trp and four Arg residues in the sequence VRRFPWWWPFLRR make this a Trp-rich cationic peptide. The structure of tritrpticin bound to membrane-mimetic sodium dodecyl sulfate micelles has been determined using conventional two-dimensional NMR methods. It forms two ...
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ژورنال
عنوان ژورنال: Biopolymers
سال: 2009
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.21071