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. 2023 Apr 21;45(4):3674–3704. doi: 10.3390/cimb45040239

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© 2023 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 (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Multiple sequence alignment of α-hairpinins: BWI-2c (UniProt P86794) from Fagopyrum esculentum; FtAMP from F. tataricum [94]; C2 (UniProt Q9ZWI3) from Cucurbita maxima; luffin P1 (UniProt P56568) from Luffa aegyptiaca; VBP-8 (PDB 6O3Q) from Solanum lycopersicum; VhTI (UniProt P85981.1) from Veronica hederifolia; MiAMP2c from Macadamia integrifolia [95]; EcAMP1 from Echinochloa crus-galli (PDB 2L2R); MBP-1 from Zea mays (UniProt P28794.1); Sm-AMP-X from Stellaria media (UniProt U4N938.1); and Tk-AMP-X from T. kiharae [96]. Cysteine residues are highlighted in white on the black background. Conserved amino acid residues are highlighted in black on the grey background. Lines above sequences denote disulfide bonds. Secondary structure elements (α-heliсеs) are shown for BWI-2c (PDB 2LQX) as helices under the alignment.