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_2115
Peptide NameCliotide T15
PMID(s)27007913
Plant Source (Scientific Name)Clitoria ternatea
Plant Source (Common Name)Asian pigeonwings
Plant FamilyFabaceae
Peptide FamilyCyclotide
Peptide FunctionAntibacterial
Peptide Function DescriptionTarget site- Lipid Bilayer; Cationic cliotides display potent antibacterial activity against Gram-negative bacteria. It also possess prominent immunostimulating activity. Cationic cliotides are capable of secretion of various cytokines and chemokines in human monocytes at both resting and lipopolysaccharide-stimulated states. Hence also used as potential candidates for novel immunomodulating therapeutics.
Activity AgainstEscherichia coli (MIC: 0.5 µM), Escherichia coli (MIC: 2.5 µM), Staphylococcus aureus, Caenorhabditis elegans
IC50 value--NA--
SequenceGLPICGETCFKTKCYTKGCSCSYPVCKRN
Sequence Length29
ValidationExperimental evidence at transcript level
Average Molecular Weight (Da)3190.79
Monoisotopic Molecular Weight (Da)3188.44
Isoelectric Point (pI)8.89
Method / ExtractionNGS, MS


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_2115


External links (Uniprot, PDB and Source Information Database)
UniprotA0A0S1RSI4
NCBI--NA--
EMBL--NA--
Link to Source DatabasesDBAASP_9052, Cybase_968, APD_02685
Addtional InformationSynthesis Type: Ribosomal; Not active up to 100 µM- Staphylococcus aureus ; Evidence for bactericidal activity- membrane disruption of E. coli. (Nguyen et al., 2016) Observed PTMs: N-terminal acetylation, de-amidation N29. (Serra et al., 2016) Highly expressed in C. ternatea root and pod. (Gilding et al., 2016); APD analysis reveals that the sequence of THE PEPTIDE shows 77.4% similarity to Cycloviolacin O15. Active against E. coli (MIC 0.5 uM).