Structure and Function of Antimicrobial Peptides
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (28 October 2019) | Viewed by 12725
Special Issue Editors
Interests: recombinant protein expression; protein structure; protein biochemistry; molecular biology; microbiology; biochemistry; nanobiotechnology; crystal structure; crystallization; microscopy
Special Issues, Collections and Topics in MDPI journals
Interests: antimicrobial peptides; membrane proteins; structural biology; protein X-ray crystallography
Interests: antimicrobial peptides; membrane proteins; structural biology; protein X-ray crystallography; efflux pumps
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
The increase in antibiotic resistance is one of the biggest health challenges our society is facing. As a consequence, the discovery of new antibiotic lead structures from all sources, including antimicrobial peptides (AMPs), is urgent. According to many recent studies, AMPs have the potential to effectively eradicate pathogenic bacteria and biofilms, and hence the potential to serve as another class of new antibiotics. However, in spite of the large number of peptides, only a minor fraction was introduced into clinical studies, and none of these is on the pharmaceutical market as new antibiotics. This is, in part, a consequence of the insufficient understanding of the mechanisms of how individual AMPs target and kill bacterial cells, and hence the rational basis for the design of new AMPs with tailored properties is impeded. Therefore, more AMP structures, ideally in complex with their cellular targets, are needed in order to track their pathways and interfaces with AMP/target-complexes so as to specifically enhance their properties.
The aim of this Special Issue is to combine the most recent developments in the structural biology, biophysics, biochemistry, and microbiology of antimicrobial peptides, focusing on a small selection of representative AMPs. This assembled information is used to reconsider the current repertoire of the three main basic AMP targeting mechanisms of bacterial cell membranes (the barrel stave model, the carpet model, and the toroidal model). The combination of the structures and functions assembled here will guide towards the architectural principles of AMPs, and give hints as to their particular mechanism targeting the molecules of the bacterial cell wall or cytoplasm, respectively. The collected information will show the diversity of molecular targets at the bacterial cell wall of Gram-positive and -negative bacteria, and will help explain why AMPs, in spite of their long evolution in the presence of bacteria, have maintained their significant activity by targeting, for example, the cytoplasmic membrane—the Achilles’ heel of the cell. Finally, the structures and functions will be used to re-formulate the three membrane-centered basic models by adding the most recent structural and functional information in order to ultimately furnish a set of new and enhanced mechanistic models, which can be used as a basis for the discussion of AMPs in future literature.
Dr. Kornelius Zeth
Dr. Håvard Jenssen
Dr. Enea Sancho-Vaello
Guest Editors
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Keywords
- Antimicrobial peptides
- Function
- Structure
- Assembly
- Fibrils, fibers, and amyloids
- Functional models
- Modelling
- Mode of action
- NMR and X-ray
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