Fragment analogs as better mimics of obestatin

ShreeRanga, Nagaraj and Muthukumar, S. Peddha and Uma, V. Manjappara (2009) Fragment analogs as better mimics of obestatin. Regulatory Peptides, 158 (1-3). pp. 143-148.

Full text not available from this repository.

Abstract

Obestatin is a twenty three amino acid peptide produced in the stomach by post translational modification of the preproghrelin gene. Since its discovery in 2005, many studies have shown that obestatin reduces feed intake and gain in body weight in rodents. Studies from our laboratory have shown the N-terminal thirteen residues mimic obestatin the best and residues 6–18 reduce epididymal fat significantly in adult male mice. In this study we have tried to increase the efficacy of these fragments. As an initial step, we have substituted G(8) with α-aminoisobutyricacid(Aib,U) and F(5) with cyclohexylalanine(Cha) in the N-terminal peptide to obtain two modified peptides and modified the middle fragment (residues 6–18) by substituting both the glycine residues at position 3 and 8 with α-aminoisobutyricacid(U). The rationale being, unusual amino acids could protect the peptides from immediate degradation and Aib would also induce secondary structure in these unstructured peptides. The N-terminal fragment with the G(8)U substitution fared the best. It reduced food intake, gain in body weight, levels of cholesterol and triglycerides in the blood, epididymal and perirenal fat in adult male mice similar to that of obestatin. The middle fragment with G(3,8)U double substitution was the second best.

Item Type:	Article
Uncontrolled Keywords:	Obestatin; N-terminal peptide; Middle fragment; α-Aminoisobutyric acid (Aib, U); Cyclohexylalanine (Cha)
Subjects:	500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 03 Amino Acid Chemistry
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	12 Nov 2010 04:01
Last Modified:	29 Jan 2018 09:48
URI:	http://ir.cftri.res.in/id/eprint/9766

Actions (login required)

View Item