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_2073	"Proteinase inhibitor PSI-1.2, HyPep"	25750185	"Capsicum annuum"	Solanaceae	"Protease inhibitor I20"	"Antifungal, Serine-protease-inhibitor"	"Target site- Lipid Bilayer; The S3 fraction showed the highest antifungal activity, inhibiting all the yeast strains tested, and it also exhibited inhibitory activity against human salivary and Callosobruchus maculatus ±-amylases as well as serine proteinases."	"Saccharomyces cerevisiae, Candida tropicalis, Candida albicans, Kluyveromyces marxianus"	KACPRNCDTDIAYMVCPSSGERIIRKVCTNCCAAQKGCKLFRSNGSIKCTGT	52	"Experimental evidence at protein level"	5603.58	5599.64	9.08	--NA--	"Synthesis Type: Ribosomal; Exhibited inhibitory activity against human salivary and Callosobruchus maculatus a-amylases and serine proteinases; 100% Inhibition against Saccharomyces cerevisiae 1038 at 25 ¼g/ml; 100% Inhibition against Candida tropicalis CE017 at 25 ¼g/ml; 65% Inhibition against Candida albicans CE022 at 25 ¼g/ml; 65% Inhibition against Kluyveromyces marxianus CE025 at 25 ¼g/ml; The sequence of this entry is 37.9% SIMILAR TO plant Tu-AMP 1 . There are four disulfide bonds: 3-32, 7-28, 16-38, and 31-49. Active again yeasts S. cerevisiae, C. albicans, C. tropicalis and K. marxianus. It also inhibited the alpha-amylase activities from C. maculatus and human saliva in vitro. This peptide S3 has an identical sequence to PSI-1.2 initially identified as serine proteinase inhibitor that inhibits both trypsin and chymotrypsin (Antcheva N et al., 2001). Also refer to UniProKB: P83241."