Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti-microbial peptides from amphibian skin
✍ Scribed by Maria Luisa Mangoni; Ludovica Marcellini H. G.; Maurizio Simmaco
- Book ID
- 105360675
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 552 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.853
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Genetically encoded cationic anti‐microbial peptides (AMPs) are essential components of the ancient and non‐specific innate immune system, which is the principal defence mechanism of all species of life, with the primary role to kill infectious microorganisms. Amphibian skin is one of the richest natural sources of such molecules, which are produced by holocrine‐type dermal glands and released upon stimulation. This review highlights the attractive and unique structural/functional properties of temporins and bombinins H, two families of short and mildly cationic peptides, isolated from the skin of frogs belonging to Rana and Bombina genera, respectively. Beside improving our knowledge on the role of AMPs in the regulation of the innate immunity, the biological significance of the existence of multiple forms of a prototypic peptide sequence within the same organism and the implication of short peptides in the endotoxin neutralization, these two classes of AMPs can be also considered as valid candidates for the design of novel anti‐infective and anti‐sepsis drugs. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.