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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Peptide S...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Peptide Science
Article . 2015 . Peer-reviewed
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Role of peptide self‐assembly in antimicrobial peptides

Authors: Xibo, Tian; Fude, Sun; Xi-Rui, Zhou; Shi-Zhong, Luo; Long, Chen;

Role of peptide self‐assembly in antimicrobial peptides

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. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.

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Keywords

Protein Stability, Molecular Sequence Data, Static Electricity, Biomedical Engineering, Peptides, Cyclic, Protein Structure, Secondary, Anti-Bacterial Agents, Nanostructures, Drug Delivery Systems, Humans, Amino Acid Sequence, Somatostatin, Hydrophobic and Hydrophilic Interactions, Antimicrobial Cationic Peptides

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    popularity
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    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
106
Top 1%
Top 10%
Top 10%
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