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Role of peptide self-assembly in antimicrobial peptides.
- Source :
-
Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2015 Jul; Vol. 21 (7), pp. 530-9. - Publication Year :
- 2015
-
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.<br /> (Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.)
- Subjects :
- Amino Acid Sequence
Biomedical Engineering
Humans
Hydrophobic and Hydrophilic Interactions
Molecular Sequence Data
Protein Stability
Protein Structure, Secondary
Somatostatin chemistry
Static Electricity
Anti-Bacterial Agents chemistry
Antimicrobial Cationic Peptides chemistry
Drug Delivery Systems methods
Nanostructures chemistry
Peptides, Cyclic chemistry
Somatostatin analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 1099-1387
- Volume :
- 21
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Journal of peptide science : an official publication of the European Peptide Society
- Publication Type :
- Academic Journal
- Accession number :
- 26100854
- Full Text :
- https://doi.org/10.1002/psc.2788