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_2001
Peptide NameSFTI-1
PMID(s)11493011, 16036912
Plant Source (Scientific Name)Helianthus annuus, Helianthus exilis, Helianthus tuberosus
Plant Source (Common Name)Common sunflower, serpentine sunflower, Jerusalem artichoke
Plant FamilyAsteraceae
Peptide FamilyBBI-like trypsin inhibitor
Peptide FunctionProtease-inhibitor, Enzymatic-digestion
Peptide Function Descriptioninhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin.
Activity Against--NA--
IC50 value--NA--
SequenceGRCTKSIPPICFPD
Sequence Length14
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)1533.82
Monoisotopic Molecular Weight (Da)1532.75
Isoelectric Point (pI)8.06
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_2001


External links (Uniprot, PDB and Source Information Database)
UniprotQ4GWU5
NCBI--NA--
EMBL--NA--
Link to Source DatabasesCybase_81, EROP-Moscow_05813
Addtional InformationBifunctional analogues of SFTI-1 found to have trypsin and chymotrypsin inhibitory activity, SFTI-1, an acyclic permutant and a [CYS-Abu]-cyclic mutant shown to possess potent trypsin inhibitory activity, nano-molar inhibitory effect against matriptase and trypsin, Both SFTI-1 and acyclic SFTI-1 are potent inhibitors of bovine beta trypsin, Bifunctional analogues of SFTI-1 found to be resistant to hydrolysis by trypsin