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- W1885513900 abstract "Antimicrobial peptides (AMPs) are considered as potential antibiotic substitutes because of their potent activities. Previous studies mainly focused on the effects of peptide charges and secondary structures, but the self-assembly of AMPs was neglected. As more and more researchers notice the roles of peptide self-assembly in AMPs, it has been considered as another important property. In this review, we will discuss the influences of peptide self-assembly on the activity and mode of action, and some specific features it introduces to the AMPs, such as particular responsiveness, improved cell selectivity and stability and sustained release. In addition, some methods to design self-assembling AMPs are primarily discussed. With further understanding about the self-assembling regularity, design of particular self-assembling AMPs will be very helpful for their applications, especially in the fields of drug delivery and biomedical engineering." @default.
- W1885513900 created "2016-06-24" @default.
- W1885513900 creator A5012324763 @default.
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- W1885513900 creator A5034813954 @default.
- W1885513900 creator A5035222788 @default.
- W1885513900 creator A5081094991 @default.
- W1885513900 date "2015-06-22" @default.
- W1885513900 modified "2023-10-10" @default.
- W1885513900 title "Role of peptide self-assembly in antimicrobial peptides" @default.
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- W1885513900 doi "https://doi.org/10.1002/psc.2788" @default.
- W1885513900 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26100854" @default.
- W1885513900 hasPublicationYear "2015" @default.
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