Abstract
The purpose of this paper is to introduce and highlight a few classes of traditional antimicrobial peptides with a focus on structure-activity relationship studies. After first dissecting the important physiochemical properties that influence the antimicrobial and toxic properties of antimicrobial peptides, the contributions of individual amino acids with respect to the peptides antibacterial properties are presented. A brief discussion of the mechanisms of action of different antimicrobials as well as the development of bacterial resistance towards antimicrobial peptides follows. Finally, current efforts on novel design strategies and peptidomimetics are introduced to illustrate the importance of antimicrobial peptide research in the development of future antibiotics.
Citation: Biljana Mojsoska and Håvard Jenssen (2015) Peptides and Peptidomimetics for Antimicrobial Drug Design Pharmaceuticals 2015, 8(3), 366-415; doi:10.3390/ph8030366
Received: 26 March 2015; Revised: 27 May 2015; Accepted: 17 June 2015; Published: 13 July 2015
Academic Editor: Guangshun Wang
Copyright: © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Concluding Remarks
There is increased evidence of emergence of bacteria resistant to conventional antibiotics illustrating the importance of research on antimicrobial drug development. Antimicrobial peptides and their synthetic derivatives hold vast potential in the development of novel antimicrobial drugs due to their (1) high biological activities; (2) low cost of production when compared with that of proteins and antibodies; (3) ease of structural modifications and stability improvements; (4) promising pharmacokinetic profiles; (5) degradation that leads to amino acids which are less toxic for the organism resulting in low immunogenicity and (6) good organ penetration.
The variety of structure-activity relationship studies for antimicrobial peptides demonstrate that the observed antibacterial activity is usually the outcome of multiple factors such as; secondary structures, amphipathicity, charge, length and hydrophobicity. The sequence composition together with the importance of specific residues and their contribution to the optimal therapeutic profiles of the peptides reveal important scaffolds for design of novel compounds to successfully combat and eliminate infectious diseases in the future.
Acknowledgments
BM holds a Ph.D. scholarship from The Danish Council for Independent Research (grant # 10-085287).
Conflicts of Interest : The authors declare no conflict of interest.
