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_2175
Peptide NameDefensin AMP2 / DmAMP2
PMID(s)7628617, 14604982, 10656585, 10931938, 13129623, 17216480
Plant Source (Scientific Name)Dahlia merckii
Plant Source (Common Name)dahlia
Plant FamilyAsteraceae
Peptide FamilyDefensin
Peptide FunctionAntibacterial, Antifungal
Peptide Function DescriptionTarget site: lipid bilayer, Dahlia merckii defensin AMP1. Cysteine-rich antimicrobial protein 1, AMPs constitute a primitive mechanism of innate immunity and help as defense to protect their hosts from microbial attack.
Activity AgainstBotrytis cinerea (IC50: 10 µg/ml), Botrytis cinerea (IC50: >100 µg/ml), Cladosporium sphaerospermum (IC50: 3 µg/ml), Cladosporium sphaerospermum (IC50: 12 µg/ml), Fusarium culmorum (IC50: 3 µg/ml), Fusarium culmorum (IC50: 12 µg/ml), Leptosphaeria maculans (IC50: 1 µg/ml), Leptosphaeria maculans (IC50: 20 µg/ml), Penicillium digitatum (IC50: 2 µg/ml), Penicillium digitatum (IC50: 50 µg/ml), Trichoderma viride (IC50: >100 µg/ml), Septoria tritici (IC50: 1 µg/ml), Septoria tritici (IC50: 2 µg/ml), Verticillium alboatrum (IC50: 2 µg/ml), Verticillium albo-atrum (IC50: >100 µg/ml)
IC50 value10 µg/ml | >100 µg/ml | 3 µg/ml | 12 µg/ml | 3 µg/ml | 12 µg/ml | 1 µg/ml | 20 µg/ml | 2 µg/ml | 50 µg/ml | >100 µg/ml | 1 µg/ml | 2 µg/ml | 2 µg/ml| >100 µg/ml
SequenceELCEKASKTWSGNCGNTGHCDNQCKSWEGAAHGACHVRNGKHMCFCYFNC
Sequence Length50
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)5525.17
Monoisotopic Molecular Weight (Da)5521.25
Isoelectric Point (pI)7.8
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_2175


External links (Uniprot, PDB and Source Information Database)
UniprotP0C8Y4
NCBI229890071
EMBL--NA--
Link to Source DatabasesDBAASP_1923, DBAASP_1922, EROP-Moscow_03014, CAMPSQ1167, APD_00918, DEFENSINS-Knowledgebase_291
Addtional InformationSynthesis Type : Ribosomal, Mature peptide: 1-50, In medium A supplemented with 1 mM CaCl2 and 50 mM KCl, the peptide is active against fungi B. cinerea (IC50 12 ug/ml), C. sphaerospermum (IC50 3 ug/ml), F. culmorum (IC50 5 ug/ml), L. maculans (IC50 1.5 ug/ml), P. digitatum (IC50 2 ug/ml), S. tritici (IC50 1 ug/ml), and V. albo-atrum (IC50 4 ug/ml) (FEBS Lett. 1995 Jul 17;368(2):257-62). It contains 4 S-S bonds. Binding of Dm-AMP1 to S. cerevisiae plasma membranes is required for antifungal activity of this protein (Mol Plant Microbe Interact. 2000;13:54-61). Specifically, it directly binds to mannosyldiinositolphosphoryl-ceramide [M(IP)2C], an acid complex sphigolipid (Thevissen K et al 2000 PNAS USA 97: 9531-6). The lack of the gene that encodes the enzyme required for the synthesis of this lipid increased resistance against Dm-AMP1. Transgenic plants: expression of this peptide in Eggplant improves resistance to pathogens (Montesinos E 2007 FEMS Microbiol Lett 270, 1-11). UPdated Jan2017.