title: Structure modeling and antidiabetic activity of a seed protein of Momordica charantia in non-obese diabetic (NOD) mice.
abstract: Momordica charantia is a well known medicinal plant used in the traditional medicinal system for the treatment of various diseases including diabetes mellitus. Recently, a novel protein termed as ADMc1 from the seed extract of M. charantia has been identified and isolated showing significant antihyperglycemic activity in type 1 diabetic rats in which diabetes was induced. However, the structure of this protein has not yet been analyzed. Homology modeling approach was used to generate a high quality protein 3D structure for the amino acid sequence of the ADMc1 protein in this study. The comparative assessment of secondary structures revealed ADMc1 as an all-alpha helix protein with random coils. Tertiary structure predicted on the template structure of Napin of B. Napus (PDB ID: 1SM7) with which the ADMc1 showed significant sequence similarity, was validated using protein structure validation tools like PROCHECK, WHAT_CHECK, VERIFY3D and ProSA. Arrangement of disulfide bridges formed by cysteine residues were predicted by the Dianna 1.1 server. The presence of multiple disulfide bond confers the stable nature of the ADMc1 protein. Further, the biological activity of the ADMc1 was assessed in non-obese diabetic (NOD) mice which are spontaneous model of type 1 diabetes. Significant reduction in the blood glucose levels of NOD mice was observed up to 8 h post administration of the rADMc1 protein. Overall, the structural characterizations with antihyperglycemic activity of this seed protein of Momordica charantia demonstrate its potential as an antidiabetic agent.
authors.affiliation: Gene Regulation Laboratory, School of Biotechnology, Jawaharlal Nehru University, New Delhi - 110067, India.
authors.forename: Gagan
authors.initials: G
authors.lastname: Chhabra
authors.forename: Aparna
authors.initials: A
authors.lastname: Dixit
keywords: Momordica charantia; homology modeling; structure validation
references.citation: Annu Rev Plant Physiol Plant Mol Biol. 1996 Jun;47:627-654
references.pmid: 15012303
references.citation: Bioinformatics. 2002 Sep;18(9):1250-6
references.pmid: 12217917
references.citation: Nucleic Acids Res. 2008 Jul 1;36(Web Server issue):W197-201
references.pmid: 18463136
references.citation: Methods Mol Biol. 2012;933:3-16
references.pmid: 22893397
references.citation: Evid Based Complement Alternat Med. 2012;2012:293650
references.pmid: 23320026
references.citation: Proteins. 1993 Dec;17(4):355-62
references.pmid: 8108378
references.citation: Planta Med. 1993 Oct;59(5):408-12
references.pmid: 8255932
references.citation: Eur J Biochem. 1987 Feb 2;162(3):485-91
references.pmid: 3830151
references.citation: Biochemistry. 2004 Dec 28;43(51):16036-45
references.pmid: 15609998
references.citation: Planta Med. 1990 Oct;56(5):426-9
references.pmid: 2077547
references.citation: J Mol Graph. 1990 Mar;8(1):52-6, 29
references.pmid: 2268628
references.citation: BMC Complement Altern Med. 2007 Sep 24;7:29
references.pmid: 17892543
references.citation: Methods Enzymol. 1997;277:396-404
references.pmid: 9379925
references.citation: Autoimmun Rev. 2007 Apr;6(5):315-22
references.pmid: 17412305
references.citation: Nucleic Acids Res. 1994 Nov 11;22(22):4673-80
references.pmid: 7984417
references.citation: Open Biochem J. 2008;2:16-28
references.pmid: 18949071
references.citation: J Ethnopharmacol. 2004 Jul;93(1):123-32
references.pmid: 15182917
references.citation: Lancet. 2009 Jun 13;373(9680):2027-33
references.pmid: 19481249