Antibacterial Peptides from Plants: What They Are and How They Probably Work
Figure 1
(a) Alignment of antibacterial peptides with defined three-dimensional structure: circulin A (1BH4); circulin B (2ERI); kalata B2 (1PT4); VrD1 (1BK8); VrD2 (2GL1); Ac-AMP2 (1MMC); brazzein (1BRZ). (b) Alignment of several antibacterial peptides from plant sources with sequences available at the Protein Data Bank. Hevein-like: Ac-AMP1 (AAB22103.1); knottin peptides: Mc-AMP1 (081338.1), Pa-AMP1 (P81418.1), Mj-AMP1 (P25403.4), Mj-AMP2 (P25404.2); snakins: snakin1 (AAD01518.1), snakin2 (ABL74292.1); defensins and thionins: pp-Thionin (P07504.1), Pth-St1 (AAB31351.1), and Cp-thionin (P84920.1); cyclotide: cyclopsychotride A (P56872.2); other peptides: MBP-1 (AAB23306.1). Asterisks show conserved cysteine residues. Sequences in bold represent peptides with cyclic three-dimensional conformations, indicating that they do not have N- and C-termini. Therefore, the alignment of cyclotides was based through comparison with the N- and C-termini of the other peptide groups.
