The DOI matches its Crossref record; 215 of the 215 references it cites were found in a registry or an index.
Antimicrobial Peptides from Plants
Open accessAbstract
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.
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Cites
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Cited by
Antimicrobial Peptides: An Update on Classifications and Databases
Bin Hafeez, A., Jiang, X., Bergen, P. J., & Zhu, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111691 · Cited by 341
Antiviral peptides as promising therapeutic drugs
Vilas Boas, L. C. P., Campos, M. L., Berlanda, R. L. A., de Carvalho Neves, N., & Franco, O. L. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03138-w · Cited by 336
Plant antimicrobial peptides: structures, functions, and applications
Li, J., Hu, S., Jian, W., Xie, C., & Yang, X. (2021) · Botanical Studies · doi:10.1186/s40529-021-00312-x · Cited by 312
Ngan, H. D., Huy, B. L., Uyen, C. L., Phuong, H. B. T., & Xuan, H. L. (2025) · European Food Research and Technology · doi:10.1007/s00217-025-04754-6 · Cited by 3
Lyapina, I., Ganaeva, D., Rogozhin, E. A., Ryabukhina, E. V., Ryazantsev, D. Y., Lazarev, V., Alieva, S. E., Mamaeva, A., & Fesenko, I. (2025) · Physiologia Plantarum · doi:10.1111/ppl.70147 · Cited by 3
Metadata
- Authors
- Tam, J., Wang, S., Wong, K., & Tan, W.
- Venue
- Pharmaceuticals
- Publisher
- MDPI AG
- Published
- 2015-11-16
- Volume
- 8
- Issue
- 4
- Pages
- 711-757
- ISSN
- 1424-8247 (ISSN-L)
- OpenAlex
- W2180208960
- Cited by
- 489
- References
- 215
- FWCI
- 23.25
- Type
- journal article
- Language
- en
- Open access
- gold
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