Isolation and characterization of peptides from momordica cochinchinensis seeds

Chan, L. Y., Wang, C. K., Major, J. M., Greenwood, K. P., Lewis, R. J., Craik, D. J. and Daly, N. L. (2009) Isolation and characterization of peptides from momordica cochinchinensis seeds. JOURNAL OF NATURAL PRODUCTS, 72 8: 1453-1458. doi:10.1021/np900174n

Author Chan, L. Y.
Wang, C. K.
Major, J. M.
Greenwood, K. P.
Lewis, R. J.
Craik, D. J.
Daly, N. L.
Title Isolation and characterization of peptides from momordica cochinchinensis seeds
Journal name JOURNAL OF NATURAL PRODUCTS   Check publisher's open access policy
ISSN 0163-3864
Publication date 2009-08
Sub-type Article (original research)
DOI 10.1021/np900174n
Volume 72
Issue 8
Start page 1453
End page 1458
Total pages 6
Editor A. Douglas Kinghorn
Place of publication Ohio, USA
Publisher American Chemical Society
Collection year 2010
Language eng
Subject C1
111205 Chemotherapy
8608 Human Pharmaceutical Products
860899 Human Pharmaceutical Products not elsewhere classified
Abstract The plant Momordica cochinchinensis has traditionally been used in Chinese medicine to treat a variety of illnesses. A range of bioactive molecules have been isolated from this plant, including peptides, which are the focus of this study. Here we report the isolation and characterization of two novel peptides, MCoCC-1 and MCoCC-2, containing 33 and 32 amino acids, respectively, which are toxic against three cancer cell lines. The two peptides are highly homologous to one another, but show no sequence similarity to known peptides. Elucidation of the three-dimensional structure of MCoCC-1 suggests the presence of a cystine knot motif, also found in a family of trypsin inhibitor peptides from this plant. However, unlike its structural counterparts, MCoCC-1 does not inhibit trypsin. MCoCC-1 has a well-defined structure, characterized mainly by a triple-stranded antiparallel β-sheet, but unlike the majority of cystine knot proteins MCoCC-1 contains a disordered loop presumably as a result of flexibility in a localized region of the molecule. Of the cell lines tested, MCoCC-1 is the most toxic against a human melanoma cell line (MM96L) and is nonhemolytic to human erythrocytes. The role of these peptides within the plant remains to be determined.
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
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Created: Fri, 05 Feb 2010, 09:05:46 EST by Susan Allen on behalf of Institute for Molecular Bioscience