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_3956
Peptide NameEAFP1
PMID(s)12067732
Plant Source (Scientific Name)Eucommia ulmoides
Plant Source (Common Name)Hardy rubber tree
Plant FamilyEucommiaceae
Peptide FamilyHevein
Peptide FunctionAntifungal
Peptide Function Description--NA--
Activity AgainstFungi: Phytophthora infestans, Ascochyta lycopersici (IC50=155 µg/mL), Verticillium dahliae, Gibberella zeae, Alternaria nicotianae, Fusarium moniliforme (IC50=56 µg/mL), Fusarium oxysporum (IC50=46 µg/mL) and Colletotrichum gossypii (IC50=35 µg/mL). Bacteria: no effect on the growth of the tested Gram-negative bacterium Bacillus megaterium and Gram-positive bacterium Pseudomonas syringae.
IC50 value155 µg/mL | 56 µg/mL | 46 µg/mL | 35 µg/mL
SequenceQTCASRCPRPCNAGLCCSIYGYCGSGNAYCGAGNCRCQCRG
Sequence Length41
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)4228.82
Monoisotopic Molecular Weight (Da)4225.66
Isoelectric Point (pI)8.62
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_3956


External links (Uniprot, PDB and Source Information Database)
UniprotP83596
NCBI32363160
EMBL--NA--
Link to Source DatabasesPhytAMP_PHYT00225, CAMPSQ351, APD_01164
Addtional InformationThe N-terminus of the peptide is blocked by pyroglutamate. This is the first finding of a plant antifungal peptide with a five-disulfide motif. The five S-S bonds are C1-C5, C2-C9, C3-C6, C4-C7, and C8-C10. EAFP1 and EAFP2 show characteristics of hevein domain and exhibit chitin-binding properties similar to the previously identified hevein-like peptides. They exhibit relatively broad spectra of antifungal activities against eight pathogenic fungi from cotton, wheat, potato, tomato and tobacco.