Literature DB >> 22074402

Antimicrobial peptides: key components of the innate immune system.

Mukesh Pasupuleti1, Artur Schmidtchen, Martin Malmsten.   

Abstract

Life-threatening infectious diseases are on their way to cause a worldwide crisis, as treating them effectively is becoming increasingly difficult due to the emergence of antibiotic resistant strains. Antimicrobial peptides (AMPs) form an ancient type of innate immunity found universally in all living organisms, providing a principal first-line of defense against the invading pathogens. The unique diverse function and architecture of AMPs has attracted considerable attention by scientists, both in terms of understanding the basic biology of the innate immune system, and as a tool in the design of molecular templates for new anti-infective drugs. AMPs are gene-encoded short (<100 amino acids), amphipathic molecules with hydrophobic and cationic amino acids arranged spatially, which exhibit broad spectrum antimicrobial activity. AMPs have been the subject of natural evolution, as have the microbes, for hundreds of millions of years. Despite this long history of co-evolution, AMPs have not lost their ability to kill or inhibit the microbes totally, nor have the microbes learnt to avoid the lethal punch of AMPs. AMPs therefore have potential to provide an important breakthrough and form the basis for a new class of antibiotics. In this review, we would like to give an overview of cationic antimicrobial peptides, origin, structure, functions, and mode of action of AMPs, which are highly expressed and found in humans, as well as a brief discussion about widely abundant, well characterized AMPs in mammals, in addition to pharmaceutical aspects and the additional functions of AMPs.

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Year:  2011        PMID: 22074402     DOI: 10.3109/07388551.2011.594423

Source DB:  PubMed          Journal:  Crit Rev Biotechnol        ISSN: 0738-8551            Impact factor:   8.429


  166 in total

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Journal:  Pathog Glob Health       Date:  2018-12-20       Impact factor: 2.894

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7.  Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.

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10.  Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells.

Authors:  Nadin Shagaghi; Andrew H A Clayton; Marie-Isabel Aguilar; Tzong-Hsien Lee; Enzo A Palombo; Mrinal Bhave
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