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. 2008 May 30;29(10):1664–1671. doi: 10.1016/j.peptides.2008.05.020

Table 1.

N-terminal sequence of kale antifungal peptide in comparison with other Brassica peptides

N-terminal sequence Reference
Kale (Brassica alboglabra) antifungal peptide 1PEGPFQGPKATKPGDLAXQTWGGWXGQTPKY31 This study
Brassica campestris antifungal peptide 1ALSCGTVSGNLAACAGYV18 [17]
Brassica napus trypsin inhibitor 1SECLKEYGGDVGFGFCAPRIYPSFCVQRC29 [5]
B. alboglabra napin-like polypeptide 4.3-kDa subunit 1PAQPFRIKK9 [21]
B. alboglabra napin-like polypeptide 7.2-kDa subunit 1RQGPFERP8 [21]

1P and Y31 indicate P and Y being the 1st and 31st residue, respectively.

Only the kale and B. campestris antifungal peptides [17] exhibit antifungal activity. The remaining two proteins [5], [21] manifest trypsin inhibitory activity. The napin-like polypeptide also possesses antibacterial and antiproliferative activities [21].