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Introduction
Antimicrobial Peptides (AMPs) are short peptides that consist of 10-50 amino acids, and were found to have antimicrobial influence on different kinds of bacteria. They are also called host defense peptides (HDPs) or defensins,Since they have different functions in their host.
AMPs are produced by Eukaryotes, as part of their defence mechanism from bacteria. They defend their host from bacteria, and also have physiological functions such as inflammation and wound healing (Wimley 2010)
Even though they have similar functions, AMPs lack any specific consensus amino acid sequences that are associated with biological activity.
History
Discovery and diversity
Structural highlights
AMPs are rich with hydrophibic (Ala, Val, Ile, Leu, Met, Phe, Tyr, Trp) and Possitively charged (Lys, Arg) Amino Acids, which seems to allow them to bind into membranes. , is a peptide from........... and it's sequence is rich with and .
AMPs have a big vareity of structures, and these structures can be divided to a few categories: alpha helix structures, beta sheet structures, and peptides with extended or loop structures.
Their structure allow them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation on the bacterial membrane .
Nevertheless, the way different antimicrobial peptides achieve their goal appears to be different, and there are a few suggested mechanisms.
Suggested Mechanisms
there are a few suggested machanisms of how AMPs work(William C. Wimley,
ACS CHEMICAL BIOLOGY, 2010). they can be divided into two:
(A) Transmembrane Pore Models of AMP Membrane Activity and (B) Nonpore Models of AMP Activity
In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that iit cannot hole it's content anymore.
Function
Disease
Relevance
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