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Peptide modulators of alpha-glucosidase
Vodnik, Miha (Author), Štempelj, Mateja (Author), Lunder, Mojca (Author), Štrukelj, Borut (Author), Molek, Peter (Author), Roškar, Irena (Author)

URLURL - Presentation file, Visit http://onlinelibrary.wiley.com/doi/10.1111/jdi.12358/epdf This link opens in a new window

Abstract
Acute glucose fluctuations during the postprandial period pose great risk for cardiovascular complications and thus represent an important therapeutic approach in type 2 diabetes. In the present study, screening of peptide libraries was used to select peptides with an affinity towards mammalian intestinal alpha-glucosidase as potential leads in antidiabetic agent development. Three phage-displayed peptide libraries were used in independent selections with different elution strategies to isolate target-binding peptides. Selected peptides displayed on phage were tested to compete for an enzyme-binding site with known competitiveinhibitors, acarbose and voglibose. The four best performing peptides were synthesized. Their binding to the mammalian alpha-glucosidase and their effect on enzyme activity were evaluated. Two linear and two cyclic heptapeptides with high affinity towards intestinal alpha-glucosidase were selected. Phage-displayed as well as synthetic peptides bind into or to the vicinity of the active site on the enzyme. Both cyclic peptides inhibited enzyme activity, whereas both linear peptides increased enzyme activity. Although natural substrates of glycosidase are polysaccharides, in the present study we successfully isolated novel peptide modulators of alpha-glucosidase. Modulatory activity of selected peptides could be further optimized through peptidomimetic design. They represent promising leads for development of efficient alpha-glucosidase inhibitors.

Language:English
Keywords:maltase glucoamylase, peptide modulators, phage display, insulin resistance, peptide libraries
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Year:2015
Number of pages:str. 625-631
Numbering:Vol. 6, iss. 6
UDC:543:615.011
ISSN on article:2040-1124
DOI:10.1111/jdi.12358 Link is opened in a new window
COBISS.SI-ID:3894385 Link is opened in a new window
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Downloads:332
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Record is a part of a journal

Title:Journal of diabetes investigation
Shortened title:J. diabetes investig.
Publisher:Wiley-Blackwell.
ISSN:2040-1124
COBISS.SI-ID:519067673 This link opens in a new window

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