Exploration of Drug Science

Table 5. Plant antimicrobial peptides.

Peptide type	Source	Structure	Mechanism of action	Examples	References
Thionins	Wheat, barley, barley seeds	Small, cysteine-rich, α/β structure	Membrane permeabilization; disruption of fungal and bacterial membranes	α-Thionin, β-thionin	[118]
Defensins	Seeds, leaves, roots	Cysteine-rich, β-sheet stabilized by disulfide bonds	Membrane disruption; inhibition of fungal and bacterial growth; broad-spectrum activity	Rs-AFP1, NaD1	[119]
LTPs	Seeds, leaves	Small, α-helical, cysteine-rich	Membrane destabilization; binds lipids; inhibits bacterial and fungal growth	LTP1, LTP2	[120]
Cyclotides	Clitoria ternatea, Viola spp.	Cyclic cystine knot peptides	Membrane disruption; high stability; broad antimicrobial activity	Kalata B1, cycloviolacin	[121]
Snakins	Potato, tomato	Cysteine-rich, helical structure	Membrane permeabilization; antifungal and antibacterial activity	Snakin-1, snakin-2	[122]
Hevein-like peptides	Hevea brasiliensis, other plants	Small, cysteine-rich peptides	Bind chitin; disrupt fungal cell walls; antifungal activity	Hevein, Ac-AMP1	[123]

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LTPs: lipid transfer proteins.

Declarations

Acknowledgments

The author thanks Graphic Era (Deemed to be University), Dehradun, India. We would like to thank Paperpal (https://paperpal.com/), Cactus Communications Services Pte Ltd., Singapore, for their invaluable online assistance in refining the language and grammar of our manuscript.

Author contributions

RK: Conceptualization, Investigation, Writing—original draft, Writing—review & editing. The author read and approved the submitted version.

Conflicts of interest

The author declares that there are no conflicts of interest.

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