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_264	Jaburetox-2Ec	--NA--	"Canavalia ensiformis"	Fabaceae	"fragment of canatoxin"	"Antifungal, Insecticidal"	--NA--	--NA--	MGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVI	93	"Experimental evidence at protein level"	10128.29	10121.85	4.48	NMR	"APD analysis reveals that the sequence of this peptide most resembles (43.6% similarity) Mj-AMP2. Mol Wt: 10098.318; mol formula: C440H690N114O147S5; GRAVY: -0.53. Its toxicity relies on an internal 10 kDa peptide (pepcanatox), released by hydrolysis of Canatoxin by cathepsins in the digestive system of susceptible insects. Shown here is the 93 amino acid fragment recombinantly expressed for biological and structural analysis (The six-residue His tag was omitted). It is insecticidal (e.g. S. frugiperda larvae). In 2012, it was shown to also inhibit fungi such as S. cerevisiae, C. parapsilosis, P. membranisfaciens at 9 uM and yeasts, C. tropicalis, K. marxiannus and C. albicans at 18 uM (Postal M et al., 2012). Membane permeation is the likely mechanism for inhibiting both insects and fungi. It seems that the N-terminal 44 residues are more important than the C-terminal portion (Martinelli AH et al., 2014). A helical region was found at the N-terminus. However, the peptide is largely diosordered, consistent with (15)N relaxation studies that revealed significant backbone mobility, especially in the N-terminal portion of the polypeptide (Lopes FC et al., 2015)."