کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1367080 | 981615 | 2007 | 5 صفحه PDF | دانلود رایگان |
Substrate analog peptides of CaMKII with varying degrees of the inhibitory potency were linked to ATPγS either by considering a phosphoryl transfer mechanism or simply by using a relatively long flexible linker. The latter bisubstrate inhibitors showed relatively little effects while the former ones improved inhibitory potency to different levels depending on the binding affinities of the peptide moieties. One of the mechanism-based bisubstrate inhibitors was then utilized to demonstrate an ATP-competitive but peptide substrate-uncompetitive inhibition, supporting an ordered binding mechanism for CaMKII.
Conjugation of AIP peptide inhibitors to ATPγS by considering a phosphoryl transfer mechanism led to improved potency in CaMKII (calmodulin-dependent protein kinase II) inhibition, which was ATP-competitive and substrate-uncompetitive.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 17, Issue 1, 1 January 2007, Pages 147–151