Structural highlights
Publication Abstract from PubMedMomordica charantia (Mc) seeds are widely used edible crop with high nutritional quality. The food and pharmaceutical industries use it as a natural anti-oxygenic agent. Herein, a ~52 kDa protein, which is a major part of seed proteome has been purified, biochemically characterized and structure has been determined. MALDI-ESI-MS identified peptide fragments and contig-deduced sequence suggested the protein to be homologous to 7S globulins. The crystal structure shows that protein has a bicupin fold similar to 7S globulins and the electron density for a copper and acetate ligand were observed in the C-terminal barrel domain. In silico study reveals that a tripeptide (VFK) from Mc7S possess a higher binding affinity for angiotensin converting enzyme (ACE) than already reported drug Lisinopril (LPR). The protein is a glycoprotein and highly stable under varying thermal and pH conditions due to its secondary structures. The DPPH (2,2-diphenyl-1-picryl-hydrazyl-hydrate) assay showed the protein to have an anti-oxygenic nature and can aid in scavenging free radical from sample. The protein can assist to enhance the nutritional and functional value of food by acting as a food antioxidant. Further, characterization of Mc7S required which might add in importance of Mc7S as antioxidant, anti-diabetic and anti-hypertensive. Structural characterization and in-silico analysis of Momordica charantia 7S globulin for stability and ACE inhibition.,Kesari P, Pratap S, Dhankhar P, Dalal V, Mishra M, Singh PK, Chauhan H, Kumar P Sci Rep. 2020 Jan 24;10(1):1160. doi: 10.1038/s41598-020-58138-9. PMID:31980708[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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