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Peptides and Peptidomimetics for Antimicrobial Drug Design
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Pharmaceuticals 2015, 8(4), 711-757; doi:10.3390/ph8040711

Antimicrobial Peptides from Plants

1
School of Biological Sciences, Nanyang Technological University, Singapore, Singapore
2
Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China
*
Author to whom correspondence should be addressed.
Academic Editor: Guangshun Wang
Received: 16 July 2015 / Revised: 6 August 2015 / Accepted: 1 September 2015 / Published: 16 November 2015
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Abstract

Plant antimicrobial peptides (AMPs) have evolved differently from AMPs from other life forms. 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, α-hairpinin and snakins family. In addition, there are AMPs which are rich in other amino acids. 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. View Full-Text
Keywords: plant antimicrobial peptides; cysteine-rich peptides; cystine knot; thionin; defensin; hevein; knottin plant antimicrobial peptides; cysteine-rich peptides; cystine knot; thionin; defensin; hevein; knottin
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Tam, J.P.; Wang, S.; Wong, K.H.; Tan, W.L. Antimicrobial Peptides from Plants. Pharmaceuticals 2015, 8, 711-757.

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