DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Kim, Sun-Chang | - |
dc.contributor.advisor | 김선창 | - |
dc.contributor.author | Park, In-Yup | - |
dc.contributor.author | 박인엽 | - |
dc.date.accessioned | 2011-12-12T07:53:41Z | - |
dc.date.available | 2011-12-12T07:53:41Z | - |
dc.date.issued | 2003 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=180986&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/27539 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생물과학과, 2003.2, [ vi, 78 p. ] | - |
dc.description.abstract | Parasin I, a 19-aa antimicrobial peptide isolated from the catfish skin, shows potent antimicrobial activity against a broad spectrum of pathogens. Therefore, to elucidate the structural features that are required for its potent antimicrobial activity and to produce parasin I analogs with increased activity, we studied the relationship between the structure and the activity of parasin I and investigated the mechanism of action of parasin I. The structure of parasin I, determined by nuclear magnetic resonance analysis, consisted of an alpha-helical region (residues 9-17) flanked by random coil regions (residues 1-8 and 18-19). To elucidate the structure-activity relationship of parasin I, we synthesized a series of N- and C-terminally truncated or amino acid-substituted synthetic parasin I analogs and examined their antimicrobial activity. Deletion of the lysine residue at the N-terminal abolished the antimicrobial activity whereas the deletion of the C-terminal random coil region slightly increased the antimicrobial potency of the peptide. Progressive deletions at the C-terminal did not cause substantial changes in antimicrobial activity of the resulting peptides until five residues were truncated whereupon the antimicrobial activity was almost completely destroyed. Regardless of helical content, a basic residue at the N-terminal was necessary for the peptides to bind to Escherichia coli cell membranes. Among the membrane-binding peptides, only those peptides with helical structure were able to permeabilize the cell membranes. Our results suggest that the lysine residue at the N-terminal mediates the binding of parasin I to the cell membrane while the helical structure of parasin I is responsible for the membrane permeabilizing activity, which kills the microorganism. A systematic approach to overcome the salt-sensitivity of parasin I was designed by the application of helix-capping motifs. The effect of helix-capping motifs on salt-sensitive antimicrobial pept... | eng |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | Antimicrobial peptide | - |
dc.subject | structure-function | - |
dc.subject | 구조-활성 | - |
dc.subject | 항균펩타이드 | - |
dc.subject | salt-resistant | - |
dc.title | Structure-function study of helical antimicrobial peptides | - |
dc.title.alternative | 나선형 항균펩타이드의 구조-활성에 관한 연구 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 180986/325007 | - |
dc.description.department | 한국과학기술원 : 생물과학과, | - |
dc.identifier.uid | 000985141 | - |
dc.contributor.localauthor | Kim, Sun-Chang | - |
dc.contributor.localauthor | 김선창 | - |
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