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 ID | PPepDB_2073 |
| Peptide Name | Proteinase inhibitor PSI-1.2, HyPep |
| PMID(s) | 25750185 |
| Plant Source (Scientific Name) | Capsicum annuum |
| Plant Source (Common Name) | Sweet and chili peppers |
| Plant Family | Solanaceae |
| Peptide Family | Protease inhibitor I20 |
| Peptide Function | Antifungal, Serine-protease-inhibitor |
| Peptide Function Description | 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. |
| Activity Against | Saccharomyces cerevisiae, Candida tropicalis, Candida albicans, Kluyveromyces marxianus |
| IC50 value | --NA-- |
| Sequence | KACPRNCDTDIAYMVCPSSGERIIRKVCTNCCAAQKGCKLFRSNGSIKCTGT |
| Sequence Length | 52 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 5603.58 |
| Monoisotopic Molecular Weight (Da) | 5599.64 |
| Isoelectric Point (pI) | 9.08 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
| Uniprot | P83241 |
| NCBI | --NA-- |
| EMBL | --NA-- |
| Link to Source Databases | DBAASP_8196, APD_02523 |
| Addtional Information | 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. |