dc.contributor.authorTam, James Pingkwan
dc.contributor.authorWang, Shujing
dc.contributor.authorWong, Ka Ho
dc.contributor.authorTan, Wei Liang
dc.date.accessioned2015-12-21T06:35:04Z
dc.date.available2015-12-21T06:35:04Z
dc.date.issued2015
dc.identifier.citationTam, J. P., Wang, S., Wong, K. H., & Tan, W. L. (2015). Antimicrobial Peptides from Plants. Pharmaceuticals, 8(4), 711-757.en_US
dc.identifier.issn1424-8247en_US
dc.identifier.urihttp://hdl.handle.net/10220/39187
dc.description.abstractPlant 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.en_US
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en_US
dc.format.extent47 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesPharmaceuticalsen_US
dc.rights© 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).en_US
dc.subjectPlant antimicrobial peptidesen_US
dc.subjectCysteine-rich peptides
dc.subjectCystine knot
dc.subjectThionin
dc.subjectDefensin
dc.subjectHevein
dc.subjectKnottin
dc.titleAntimicrobial Peptides from Plantsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.3390/ph8040711
dc.description.versionPublished versionen_US


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