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 |
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| PPepDB ID | PPepDB_2214 |
| Peptide Name | Kalata-B1 |
| PMID(s) | 21928440, 10430870, 21723349, 21576247, 28669767, 11535828, 7703226, 10430870, 11888199, 12482862, 12482868, 12779323, 17534989 |
| Plant Source (Scientific Name) | Oldenlandia affinis, Viola yedoensis |
| Plant Source (Common Name) | Blue Diamond Flower |
| Plant Family | Rubiaceae, Violaceae |
| Peptide Family | Cyclotide |
| Peptide Function | Antibacterial, Antifungal, Antiviral, Anticancer, Hemolytic, Cytotoxic, Nematocide, Molluscicidal, Membrane-Binding, Metal-binding, Insecticidal, Enzymatic-digestion, Anti-HIV, Enzyme-inhibitor |
| Peptide Function Description | The Kalata B1 showed significant activity in inhibiting development of nematode larvae and motility of adult worms; The existing diversity of cyclotides in plants could be used to develop natural molluscicides; Have the capability to alter membrane permeability leading to the loss of the internal vesicle contents to the external medium; Help in screening the selective binding of putative antimicrobial peptides to model mammalian or microbial phospholipid membranes; Kalata B1 binds to Mn2 in the presence of DPC micelles; Kalata B1 shown to possess potent insecticidal activity; G6A and E7A mutants of kalata B1 were completely impervious to enzymatic digestion; Shown to possess potent anti-HIV activity; Kalata B1 shown to possess some anti-bacterial activity.; Target site: lipid bilayer; 50% Hemolysis & 41% Hemolysis against Human erythrocytes at 26 & 25 µM; Human foreskin fibroblasts HFF-1(IC50: 2.38 ±0.09 µM) |
| Activity Against | Escherichia coli (MIC: >500 µM), Pseudomonas aeruginosa (MIC: >500 µM), Proteus vulgaris (MIC: >500 µM), Klebsiella oxytoca (MIC: 54.8 µM), Staphylococcus aureus (MIC: 0.26 µM), Micrococcus luteus (MIC: 40.4 µM), Candida albicans (MIC: >500 µM), Candida kefyr (MIC: 21.4 µM), Candida tropicalis (MIC: >500 µM), Human skin melanoma MM96L(IC50: 3.10 ±0.06 µM), Human cervical carcinoma HeLa(IC50: 10.21 ±0.43 µM), Human gastric cancer BGC-823(IC50: 1.32 ±0.15 µM), Escherichia coli (MBC50: 40 µM), Escherichia coli (MBC99: 80 µM), Escherichia coli (MIC: >160 µM), Pseudomonas aeruginosa (MBC50: 2.5 µM), Pseudomonas aeruginosa (MBC99: 10 µM), Pseudomonas aeruginosa (MIC: 40 µM), Pseudomonas aeruginosa (MIC: >160 µM), Staphylococcus aureus (MBC50: 160 µM), Staphylococcus aureus (MBC99: >160 µM), Staphylococcus aureus (MIC: >160 µM), Candida albicans (MFC50: >160 µM), Candida albicans (MFC99: >160 µM), Candida albicans (MIC: >160 µM), Human histiocytic lymphoma U-937/GTB(IC50: 6.9 µM ) |
| IC50 value | 3.10 ±0.06 µM | 10.21 ±0.43 µM | 1.32 ±0.15 µM | 6.9 µM |
| Sequence | GLPVCGETCVGGTCNTPGCTCSWPVCTRN |
| Sequence Length | 29 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 2916.34 |
| Monoisotopic Molecular Weight (Da) | 2914.2 |
| Isoelectric Point (pI) | 5.96 |
| Method / Extraction | PcR, NGS, MS, EST, Amino acid analysis |
| External links (Uniprot, PDB and Source Information Database) |
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| Uniprot | Q5USN7, B6E618, B5B3Z3, B5B3Z7, B6E615, D8WS41, P56254 |
| NCBI | --NA-- |
| EMBL | --NA-- |
| Link to Source Databases | DBAASP_734, DBAASP_5392, PhytAMP_PHYT00189, EROP-Moscow_03433, EROP-Moscow_07304, EROP-Moscow_07303, EROP-Moscow_14275, Cybase_1, CAMPSQ2869, APD_00729 |
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| Addtional Information | First isolated by Gran in 1973 (Acta Pharmacol Toxicol (Copenh). 1973;33(5):400-8), the circular structure was established in 1995 (Saether O, et al.), and antimicrobial activity was demonstrated in 1999, thereby establishing it as an AMP. Cellular location: accumulated in vacuole and processed likely by asparaginyl endoproteinase (Conlan BF et al. 2011 Am J Bot 98:2018-26). Structure: there are other PDB entries: 1JJZ, 1NB1, and 1ZNU. You can rotate, zoom, and view the 4TTM structure here in the PDB . Antibacterial activity was salt dependent and the peptide was most active against S. aureus (0.26 uM). The overall fold is important for anti-HIV activity, since the acyclic permutant is inactive. Kalata B1 also has uterotonic and insecticidal activity (natural pesticide). (MOA) An all D-analog is also active, supporting membrane targeting (Sando L. et al. 2011 Chembiochem 12: 2456-62). NMR studies of the ternary complex identified amino acid residues in loop 5 (W23, P24, and V25) and loop 6 (L2, P3, and V4) are important for membrane binding (Shenkarrev ZO et al. 2006 FEBS J 273:2658-72). It binds to phosphatidylethanolamine and leads to pore formation (41-70 A) in lipid bilayers (Huang et al 2009 JBC 284: 20699-20707). Oligomerization on the membrane surface could be important for this process. Note that oxidized forms of this peptide have also been reported. Trp can be oxidized to oxindolylalanine I (oia) or N-formylkynurenine (nfk). The effect of such oxidation on activity is unknown (Plan MR et al 2007 Chembiochem 8:1001-11). It also inhibits the human prolyl oligopeptidase (POP) (Hellinger R et al., 2015). Updated 1/15/2010; 11/9/2011; 1/5/2012; 3/25/2012; reference updated 5/1/2013; 2/2016. | circular structure; G6 is critical to bind phosphatidylethanolamine (Hall et al., 2012 Biochim Biophys Acta 1818:2354).; Synthesis Type : Ribosomal| Modifying the Arg with a keto aldehyde significantly reduced its activity against S.aureus. Two-disulfide synthetic variants exhibited antimicrobial profiles similar to the native peptide. |
