Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 정병문 | * |
dc.date.accessioned | 2016-08-27T04:08:03Z | - |
dc.date.available | 2016-08-27T04:08:03Z | - |
dc.date.issued | 2016 | * |
dc.identifier.issn | 1525-7797 | * |
dc.identifier.issn | 1526-4602 | * |
dc.identifier.other | OAK-16666 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/218122 | - |
dc.description.abstract | There ate four EF-hand polypeptides in calmodulin, a natural ubiquitous calcium binding protein that activates the enzymes involved in Ca2+-mediated signal transduction. An EF-hand polypeptide has six carboxylate functional groups in the middle loop region between two rigid polypeptides. In this study, a calcium binding polymer (CBP) with a structure of poly(L-alanine)-poly(L-alanine-co-L-glutamic acid)-poly(ethylene glycol)-poly(L-alanine-co-L-glutamic acid)-poly(L-alanine) (PA-PAE-PEG-PAE-PA; A(11.1)-A(3.4)E(3.2)-EG(40.1)-A(3.4)E(3.2)-A(11.1)) was synthesized by mimicking the EF-hand polypeptide. The 6-7 carboxylate functional groups from PAE are expected to form a binding site for Ca2+. As the Ca2+ bound to CBP, small changes in the circular dichroism spectra and C-13 NMR spectra were observed, indicating that Ca2+ binding to CBP induced changes in the conformation of CBP. The binding constant of CBP to Ca2+ was investigated by using the competitive binding of 2,2',2 '',2'''-{ethane-1,2,diylbis[oxy(4-bromo-2,1-phenylene)nitrilo]} tetraacetie acid (5,5-Br-2-BAPTA). The binding constant obtained with a CaLigator program by least-squares fitting of the absorbance profile as a function of Ca2+ concentration was 5.1 X 10(5) M-1, which was similar to that of calmodulin. The selectivity of CBP for metal ion binding was compared among Ca2+, Cu2+, and Zn2+. The binding constant was obtained through. a similar competitive binding study with murexide. The binding constants for Ca2+, Cu2+, and Zn2+ were 7.0 X 10(5), 4.2 X 10(5), and 1.7 X 10(5) respectively, indicating 2-4 fold higher selectivity of CBP for Ca2+ compared to Cu2+ and Zn2+. The,CBP has selectivity for Ca2+, and binding affinity for Ca2+ was similar to the biological Ca2+ binding motif of calmodulin. | * |
dc.language | English | * |
dc.publisher | AMER CHEMICAL SOC | * |
dc.title | EF-Hand Mimicking Calcium Binding Polymer | * |
dc.type | Article | * |
dc.relation.issue | 3 | * |
dc.relation.volume | 17 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 1075 | * |
dc.relation.lastpage | 1082 | * |
dc.relation.journaltitle | BIOMACROMOLECULES | * |
dc.identifier.doi | 10.1021/acs.biomac.5b01694 | * |
dc.identifier.wosid | WOS:000372391800039 | * |
dc.identifier.scopusid | 2-s2.0-84961219246 | * |
dc.author.google | Chung, Hee Jung | * |
dc.author.google | Ko, Du Young | * |
dc.author.google | Moon, Hyo Jung | * |
dc.author.google | Jeong, Byeongmoon | * |
dc.contributor.scopusid | 정병문(7102237959) | * |
dc.date.modifydate | 20240118155902 | * |