Peptides binding to the hunger hormone ghrelin
Vodnik, Miha (Author), Molek, Peter (Author), Štrukelj, Borut (Author), Lunder, Mojca (Author)

URLURL - Presentation file, Visit https://www.thieme-connect.com/ejournals/abstract/10.1055/s-0032-1331744 This link opens in a new window

The neutralisation of circulating ghrelin, the only known peripheral orexigenic peptide hormone, is a promising approach for the pharmacological treatment of obesity. To select peptides with an affinity towards ghrelin, 4 selection procedures were carried out with random peptide phage display libraries Ph.D.-7 and Ph.D.-12. Due to the absence of a common consensus motif, a stepwise elimination approach was used. The pool of selected peptides displaying phage clones was thoroughly examined to remove any potential target-unrelated peptides. The affinity of the remaining phage clones for ghrelin was tested with ELISA. An analysis of the binding properties revealed four-phage displayed peptides that bind to ghrelin with moderate affinity, with ADTVPRH and MEMKKTHPVLGA being the most specific. Additional advantage of peptide MEMKKTHPVLGA is an indication of binding to octanoyl group on N-terminal part of ghrelin, involved in receptor interaction. Hence peptide MEMKKTHPVLGA represents the most suitable lead for further investigation.

Keywords:ghrelin, des-acyl ghrelin, phage display, neutralising peptides
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Number of pages:str. 372-377
Numbering:Vol. 45, no. 5
ISSN on article:0018-5043
DOI:10.1055/s-0032-1331744 Link is opened in a new window
COBISS.SI-ID:3398513 Link is opened in a new window
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Record is a part of a journal

Title:Hormone and Metabolic Research
Shortened title:Horm. Metab. Res.
Publisher:Thieme-Stratton, Thieme
COBISS.SI-ID:25570304 This link opens in a new window

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