Detailed Peptide Information


This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking



Primary Information
PPepDB IDPPepDB_2073
Peptide NameProteinase inhibitor PSI-1.2, HyPep
PMID(s)25750185
Plant Source (Scientific Name)Capsicum annuum
Plant Source (Common Name)Sweet and chili peppers
Plant FamilySolanaceae
Peptide FamilyProtease inhibitor I20
Peptide FunctionAntifungal, Serine-protease-inhibitor
Peptide Function DescriptionTarget 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.
Activity AgainstSaccharomyces cerevisiae, Candida tropicalis, Candida albicans, Kluyveromyces marxianus
IC50 value--NA--
SequenceKACPRNCDTDIAYMVCPSSGERIIRKVCTNCCAAQKGCKLFRSNGSIKCTGT
Sequence Length52
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)5603.58
Monoisotopic Molecular Weight (Da)5599.64
Isoelectric Point (pI)9.08
Method / Extraction--NA--


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_2073


External links (Uniprot, PDB and Source Information Database)
UniprotP83241
NCBI--NA--
EMBL--NA--
Link to Source DatabasesDBAASP_8196, APD_02523
Addtional InformationSynthesis 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.