Antimicrobial peptides bind more strongly to membrane pores
نویسندگان
چکیده
منابع مشابه
Toroidal pores formed by antimicrobial peptides show significant disorder.
A large variety of antimicrobial peptides have been shown to act, at least in vitro, by poration of the lipid membrane. The nanometre size of these pores, however, complicates their structural characterization by experimental techniques. Here we use molecular dynamics simulations, to study the interaction of a specific class of antimicrobial peptides, melittin, with a dipalmitoylphosphatidylcho...
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Antimicrobial peptides (AMPs) are promising next generation antibiotics that hold great potential for combating bacterial resistance. AMPs can be both bacteriostatic and bactericidal, induce rapid killing and display a lower propensity to develop resistance than do conventional antibiotics. Despite significant progress in the past 30 years, no peptide antibiotic has reached the clinic yet. Poor...
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Peptide-induced pore formation in membranes can be dissected into two steps: pore formation and peptide binding to the pore. A computational method is proposed to study the second step in anionic membranes. The electrostatic potential is obtained from numerical solutions to the Poisson-Boltzmann equation and is then used in conjunction with IMM1 (implicit membrane model 1). A double charge laye...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2010
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2010.02.023