Antimicrobial Peptides. AMPs are widely distributed throughout nature and have been discovered in certain bacteria, protozoa, fungi, plants, and multicellular. They are generally rich in cysteine residues which form multiple disulfides. In turn, the disulfides cross- braced plant AMPs as cystine- rich peptides to confer them with extraordinary high chemical, thermal and proteolytic stability. The cystine- rich or commonly known as cysteine- rich peptides (CRPs) of plant AMPs are classified into families based on their sequence similarity, cysteine motifs that determine their distinctive disulfide bond patterns and tertiary structure fold. Cystine- rich plant AMP families include thionins, defensins, hevein- like peptides, knottin- type peptides (linear and cyclic), lipid transfer proteins, . In addition, there are AMPs which are rich in other amino acids. An antimicrobial is an agent that kills microorganisms or inhibits their growth. Antimicrobial medicines can be grouped according to the microorganisms they act.
The ability of plant AMPs to organize into specific families with conserved structural folds that enable sequence variation of non- Cys residues encased in the same scaffold within a particular family to play multiple functions. Furthermore, the ability of plant AMPs to tolerate hypervariable sequences using a conserved scaffold provides diversity to recognize different targets by varying the sequence of the non- cysteine residues. These properties bode well for developing plant AMPs as potential therapeutics and for protection of crops through transgenic methods. This review provides an overview of the major families of plant AMPs, including their structures, functions, and putative mechanisms. Antimicrobial peptides encompass a wide variety of structural motifs. The majority of these peptides are cationic and.
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December 2016
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