PPepDB-ID	"Peptide Name"	PMID	"Plant source"	"Plant Family"	"Peptide Family"	"Peptide function"	"Peptide function description"	"Activity against"	Sequence	"Sequence Length"	Validation	"Avg. Molecular wt(Da)"	"Monoisotopic molecular wt(Da)"	pI	Method	"Additional information"
PPepDB_3852	WAMP-1b	"25154438, 19583772"	"Triticum kiharae"	Poaceae	--NA--	"Antimicrobial, Antifungal"	"This block the fungalysin activity, keeping the chitinase intact. Thus, WAMPs represent novel protease inhibitors that are active against fungal metalloproteases. WAMPs directly inhibited hyphal elongation, and plays an important role in fungal development. Degradation of chitin cell wall."	"F. verticillioides (IC50=2.7 ±0.15M)"	AQRCGDQARGAKCPNCLCCGKYGFCGSGDAYCGAGSCQSQCRGCR	45	"Experimental evidence at protein level"	4601.21	4597.83	8.62	--NA--	"Compared to WAMP-1a, WAMP-1b contains one additional Arg at the C-terminus. 10-Cys. MOA: This proteinase of fungi (fungalysin Fv-cmp) cleaves class IV chitinases, plant defense proteins that bind and degrade chitin of fungal cell walls. However, equal molar ratio of plant defensin WAMP-1b or WAMP-2 to chitinase was sufficient to block the fungalysin activity of fungi keeping the plant chitinase intact. Thus, WAMPs represent a novel type of protease inhibitors (enzyme inhibitor) being active against fungal metalloproteases (Slavokhotova etal., 2014). UPdated 8/2014."