Structural Studies of Copper(II)-Hippuryl-L-histidyl-L-leucine(HHL) Complex by NMR Methods
- Authors
- 이성란; 전지현; 원호식
- Issue Date
- Jun-2006
- Publisher
- 한국자기공명학회
- Keywords
- HHL; Complex; NMR
- Citation
- Journal of the Korean Magnetic Resonance Society, v.10, no.1, pp.115 - 125
- Indexed
- KCI
OTHER
- Journal Title
- Journal of the Korean Magnetic Resonance Society
- Volume
- 10
- Number
- 1
- Start Page
- 115
- End Page
- 125
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/45231
- ISSN
- 1226-6531
- Abstract
- Hippuryl-L-histidyl-L-leucine(HHL) is widely used as a substrate of angiotensin converting enzyme(ACE) cleaving the neurotransmitter angiotensin(I) to the octapeptide angiotensin(II). The structure of the substrate molecules should provide information regarding the geometric requirements of the ACE active site. For the purpose of determination of in vivo reaction, metallo(Cu, Zn)-HHL complexes were synthesized and the degree of complex formation were identified by MALDI-TOF, ESI mass spectrometric analysis. In addition, the pH-dependent species distribution curves were obtained by potentiometric titration. Nitrogen atoms of imidazole ring and oxygen atom of caboxylate groups in the peptide chain were observed to be participated in the metal complex formation. After purification of complexes further structural characterization were made by utilizing UV-Vis, electrochemical methods and NMR. Complete NMR signal assignments were carried out by using 2D-spectrum techniques COSY, TOCSY, NOESY, HETCOR. A complex that two imidazole and carboxylate groups are asymmetrically participating to coordination mode was predicted to the solution-state structure of Cu(II)-HHL2 based on 13C-NMR signal assignment and NOE information
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Collections - COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY > DEPARTMENT OF CHEMICAL AND MOLECULAR ENGINEERING > 1. Journal Articles
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