ArticleBioorganic & medicinal chemistry2010
The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine.
Article in Bioorganic & medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin.PloS one · 2015Article
- Structural characterization of intrinsically disordered proteins by NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- Solution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probes.Molecules (Basel, Switzerland) · 2013Review
- Ghrelin receptors in non-Mammalian vertebrates.Frontiers in endocrinology · 2013Article
- Acylation type determines ghrelin's effects on energy homeostasis in rodents.Endocrinology · 2012Article
- Determining the orientation and localization of membrane-bound peptides.Current protein & peptide science · 2012Review
- Article
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4 authors.
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Abstract
The peptide hormone ghrelin, which is the natural ligand of the membrane-bound growth hormone secretagogue receptor (GHS-R), regulates overall body and cell growth, energy homeostasis, carbohydrate, protein and lipid metabolism and water electrolyte balance. It contains an O-acyl linked octanoyl group on Ser3 and is the only peptide known to contain such a modification. Using solution state NMR spectroscopy and ultrafiltration we found that human ghrelin binds to membrane-mimetic environments via its octanoyl group as well as the aromatic moiety of Phe4. Relaxation enhancements in a paramagnetic environment reveal that both the octanoyl group on Ser3 and the aromatic group on Phe4 are inserted deep into the hydrophobic core of phosphocholine assemblies while the remaining peptide is freely mobile in solution. In contrast, no binding was observed for des-octanoyl ghrelin. Thus, the octanoyl chain, together with the Phe4 aromatic group of ghrelin, functions as a membrane anchor. Our results are in parallel with the previous finding that a bulky hydrophobic group on Ser3 and Phe4 of ghrelin are necessary for its function and thus indicate that membrane-binding is essential for ghrelin function.
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