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Varv peptide E

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Varv peptide E is a macrocyclic polypeptide isolated from Viola arvensis.

Category
Functional Peptides
Catalog number
BAT-010930
Synonyms
Gly-Leu-Pro-Ile-Cys-Gly-Glu-Thr-Cys-Val-Gly-Gly-Thr-Cys-Asn-Thr-Pro-Gly-Cys-Ser-Cys-Ser-Trp-Pro-Val-Cys-Thr-Arg-Asn
Sequence
cyclo-(TCVGGTCNTPGCSCSWPVCTRNGLPICGE)
1. Cycloviolins A-D, anti-HIV macrocyclic peptides from Leonia cymosa
Y F Hallock, R C Sowder 2nd, L K Pannell, C B Hughes, D G Johnson, R Gulakowski, J H Cardellina 2nd, M R Boyd J Org Chem. 2000 Jan 14;65(1):124-8. doi: 10.1021/jo990952r.
Four novel anti-HIV macrocyclic peptides containing 28-31 amino acid residues, named cycloviolins A-D, have been isolated from the hitherto unstudied tropical plant Leonia cymosa. Their primary structure, including amino acid composition and sequence, was determined by a combination of MALDI-TOF and FAB MS and by enzymatic digestion of reduced derivatives, followed by Edman degradation and mass analyses. All of the cycloviolins contain six cysteines, which are present as three intramolecular disulfide bridges. Intriguingly, cycloviolins A-D showed high degrees of sequence homology to the known cyclopsychotride A and circulins A and B from the Rubiaceae family but much less homology to the varv peptides from Viola, a member of the same family (Violaceae).
2. Cytotoxic cyclotides from Viola tricolor
Erika Svangård, Ulf Göransson, Zozan Hocaoglu, Joachim Gullbo, Rolf Larsson, Per Claeson, Lars Bohlin J Nat Prod. 2004 Feb;67(2):144-7. doi: 10.1021/np030101l.
A crude fraction of Viola tricolor rich in small lipophilic proteins was prepared and subjected to fractionation guided by bioactivity, using RP-HPLC and a fluorometric cytotoxicity assay. Two human cancer cell lines, U-937 GTB (lymphoma) and RPMI-8226/s (myeloma), were used in this study. The most potent compounds isolated, that is, the compounds showing the lowest IC(50) values, were shown to be three small proteins: vitri A (IC(50) = 0.6 microM and IC(50) = 1 microM, respectively), varv A (IC(50) = 6 microM and IC(50) = 3 microM, respectively), and varv E (IC(50) = 4 microM in both cell lines). Their sequences, determined by automated Edman degradation, quantitative amino acid analysis, and mass spectrometry, were cyclo-GESCVWIPCITSAIGCSCKSKVCYRNGIPC (vitri A), cyclo-GETCVGGTCNTPGCSCSWPVCTRNGLPVC (varv A), and cyclo-GETCVGGTCNTPGCSCSWPVCTRNGLPIC (varv E), of which vitri A is described for the first time. Each forms a head-to-tail cyclic backbone, with six cysteine residues being involved in three disulfide bonds, characteristic of the family of small proteins called the cyclotides. This is the first report on cyclotides from the species V. tricolor and the first report on the sequence of the cytotoxic cyclotide vitri A.
3. Primary and 3-D modelled structures of two cyclotides from Viola odorata
Erika Svangård, Ulf Göransson, Derek Smith, Chandra Verma, Anders Backlund, Lars Bohlin, Per Claeson Phytochemistry. 2003 Sep;64(1):135-42. doi: 10.1016/s0031-9422(03)00218-8.
Two polypeptides named vodo M and vodo N, both of 29 amino acids, have been isolated from Viola odorata L. (Violaceae) using ion exchange chromatography and reversed phase HPLC. The sequences were determined by automated Edman degradation, quantitative amino acid analysis, and mass spectrometry (MS). Using MS, it was established that vodo M (cyclo-SWPVCTRNGAPICGESCFTGKCYTVQCSC) and vodo N (cyclo-SWPVCYRNGLPVCGETCTLGKCYTAGCSC) form a head-to-tail cyclic backbone and that six cysteine residues are involved in three disulphide bonds. Their origin, sequences, and cyclic nature suggest that these peptides belong to the family of cyclic plant peptides, called cyclotides. The three-dimensional structures of vodo M and vodo N were modelled by homology, using the experimentally determined structure of the cyclotide kalata B1 as the template. The images of vodo M and vodo N show amphipathic structures with considerable surface hydrophobicity for a protein modelled in a polar environment.
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