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• W2164329199 abstract "Simulations of antimicrobial peptides in membrane mimics can provide the high resolution, atomistic picture that is necessary to decipher which sequence and structure components are responsible for activity and toxicity. With such detailed insight, engineering new sequences that are active but non-toxic can, in principle, be rationalized. Armed with supercomputers and accurate force fields for biomolecular interactions, we can now investigate phenomena that span hundreds of nanoseconds. Although the phenomena involved in antimicrobial activity, (i.e., diffusion of peptides, interaction with lipid layers, secondary structure attainment, possible surface aggregation, possible formation of pores, and destruction of the lipid layer integrity) collectively span time scales still prohibitively long for classical mechanics simulations, it is now feasible to investigate the initial approach of single peptides and their interaction with membrane mimics. In this article, we discuss the promise and the challenges of widely used models and detail our recent work on peptide–micelle simulations as an attractive alternative to peptide–bilayer simulations. We detail our results with two large structural classes of peptides, helical and beta-sheet and demonstrate how simulations can assist in engineering of novel antimicrobials with therapeutic potential." @default.
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• W2164329199 date "2006-09-01" @default.
• W2164329199 modified "2023-10-11" @default.
• W2164329199 title "Driving engineering of novel antimicrobial peptides from simulations of peptide–micelle interactions" @default.
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• W2164329199 doi "https://doi.org/10.1016/j.bbamem.2006.03.010" @default.
• W2164329199 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2860964" @default.
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