Molecular Interaction between kisspeptin decapeptide analogs and a lipid membrane
- Authors
- Lee, Ju Yeon; Moon, Jung Sun; Eu, Young-Jae; Lee, Chul Won; Yang, Sung-Tae; Lee, Seung Kyu; Jung, Hyun Ho; Kim, Ha Hyung; Rhim, Hyewhon; Seong, Jae Young; Kim, Jae Il
- Issue Date
- 15-5월-2009
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Kisspeptin; GPR54; Peptide-membrane interaction; NMR; DPC
- Citation
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.485, no.2, pp.109 - 114
- Indexed
- SCIE
SCOPUS
- Journal Title
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Volume
- 485
- Number
- 2
- Start Page
- 109
- End Page
- 114
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/120050
- DOI
- 10.1016/j.abb.2009.03.002
- ISSN
- 0003-9861
- Abstract
- Kisspeptin-10 is the C-terminal decapeptide amide of kisspeptin, in endogenous ligand for GPR54, and exhibits the same binding and agonist activity as the parent molecule. Although GPR54 is a membrane-embedded protein, details of the molecular interaction between kisspeptin-10 and lipid membranes remain unclear. Here, we performed a series of structural analyses using alanine-scanning analogs of kisspeptin-10 in membrane-mimetic medium. We found that there is a close correlation between lipid membrane binding and agonist activity. For instance, the F10A and non-amidated (NH2 -> OH) analogs showed little or no GPR54-agonist activity and elicited 110 I)blue shift in tryptophan fluorescence. NMR analysis of kisspeptin-10 analog in DPC micelles revealed it to contain several tight torn structures. encompassing residues Trp3 to Phe 10, bur no helical conformation like that seen previously with SDS micelles. Together, our results suggest that kisspeptin-10 may activate GPR54 via a ligand transportation Pathway incorporating a lipid membrane. (C) 2009 Elsevier Inc. All rights reserved.
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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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