Preparation, characterization and kinetic study of the β-cyclodextrin-based artificial metalloenzymesβ-Cyclodextrin을 이용한 artificial metalloenzyme의 제조와 특성 연구

Cited 0 time in webofscience Cited 0 time in scopus
  • Hit : 569
  • Download : 0
DC FieldValueLanguage
dc.contributor.advisorByun, Si-Myung-
dc.contributor.advisor변시명-
dc.contributor.authorJeon, Won-Bae-
dc.contributor.author전원배-
dc.date.accessioned2011-12-12T07:52:25Z-
dc.date.available2011-12-12T07:52:25Z-
dc.date.issued1999-
dc.identifier.urihttp://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=151527&flag=dissertation-
dc.identifier.urihttp://hdl.handle.net/10203/27456-
dc.description학위논문(박사) - 한국과학기술원 : 생물과학과, 1999, [ v, 88 p. ]-
dc.description.abstractMetal ions are essential participants for the catalytic activities or structural stabilities of metalloenzymes. Metalloenzymes use the cooperative action between the substrate binding site and catalytic metal center. β-Cyclodextrin is a naturally occurring cyclic heptamer of D-(+)-glucopyranose units that are linked by $\alpha$(1→4) glucopyranose bonds. In this study, new supramolecular β-CD monomer 1 in which Cu(Ⅱ) ion binding sites are attached to the primary side of hydrophobic β-CD pockets, was prepared. β-CD dimers possessing tridentate 7- (2), pentadentate 13- (3) and 15-membered (4) pyridine diamide chelators were designed, synthesized and characterized by MALDI-MS, NMR, IR and UV-Visible spectroscopy. Fluorescence and pH-metric titration were carried out in order to ascertain their behavior as bifunctional hosts for fluorescence guests and metal ions. As expected, supramolecular β-CD dimers have high binding affinity for fluorescence guests, e.g. TNS and TPPS. Supramolecular β-CD monomer and dimers chelate Cu(Ⅱ) ion by forming amidate-Cu(Ⅱ) complexes. The $pK_{a1}$ values for the Cu(Ⅱ) promoted deprotonation of amide ligands from 1, 3 and 4 were determined to be 4.3, 6.3 and 6.3, respectively. Above pH 8.0, supramolecular ligands 3 and 4 bind fluorescent guest and Cu(Ⅱ) ion simultaneously. 1-Cu(Ⅱ), 3-Cu(Ⅱ) and 4-Cu(Ⅱ) complexes were isolated as blue or purple solids. Cu(Ⅱ) complexes catalyze the hydrolysis of p-nitrophenyl acetate, adamantate and amino acids in an enzyme-like manner; displaying Michaelis-Menten kinetics, substrate specificity and competitive inhibition. In this context, these complexes are regarded as artificial metalloenzyme. Artificial metalloenzymes hydrolyze the p-nitrophenyl esters by the nucleophilic addition of a Cu(Ⅱ)-coordinated hydroxide ion to the carbonyl carbon of substrate included in hydrophobic β-CD pocket. These results support the zinc hydroxide mechanism of carboxypeptidase A.eng
dc.languageeng-
dc.publisher한국과학기술원-
dc.subjectβ-cyclodextrin-
dc.subjectMetalloenzyme-
dc.subject메탈로엔자임-
dc.subject베타싸이클로덱스트린-
dc.titlePreparation, characterization and kinetic study of the β-cyclodextrin-based artificial metalloenzymes-
dc.title.alternativeβ-Cyclodextrin을 이용한 artificial metalloenzyme의 제조와 특성 연구-
dc.typeThesis(Ph.D)-
dc.identifier.CNRN151527/325007-
dc.description.department한국과학기술원 : 생물과학과, -
dc.identifier.uid000945379-
dc.contributor.localauthorByun, Si-Myung-
dc.contributor.localauthor변시명-
Appears in Collection
BS-Theses_Ph.D.(박사논문)
Files in This Item
There are no files associated with this item.

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0