Ahn, Dae-Ro Han, Ki-Cheol Kwon, Hyuk Sung Yang, Eun Gyeong 2024-01-21T01:35:00Z 2024-01-21T01:35:00Z 2021-09-05 2007-01-01 0960-894X https://pubs.kist.re.kr/handle/201004/134750 Substrate analog peptides of CaMKII with varying degrees of the inhibitory potency were linked to ATP gamma S 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 (c) 2006 Elsevier Ltd. All rights reserved. English PERGAMON-ELSEVIER SCIENCE LTD MULTISUBSTRATE ANALOG INHIBITORS DESIGN MECHANISM BINDING DOMAIN ATP-conjugated peptide inhibitors for calmodulin-dependent protein kinase II Article 10.1016/j.bmcl.2006.09.070 1 BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, v.17, no.1, pp.147 - 151 BIOORGANIC & MEDICINAL CHEMISTRY LETTERS 17 1 147 151 scie scopus 000243630500028 2-s2.0-33845675624 Chemistry, Medicinal Chemistry, Organic Pharmacology & Pharmacy Chemistry Article MULTISUBSTRATE ANALOG INHIBITORS DESIGN MECHANISM BINDING DOMAIN bisubstrate analog inhibitors ATP-conjugated peptide inhibitors calmodulin-dependent protein kinase II