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Characterization of the unique function of self aggregation and disulfide dimerization of the peptdie with membrane permeability
지질막 투과성을 가지는 펩타이드의 자기 결합과 이중화의 독특한 특성 파악
초록
We identified an active fragment from tenecin 1, an insect defensin protein. Interestingly, the active fragment that had unique primary structure containing three cys residues did not show antimicrobial activity dependent on the presence of DTT. To understand the mode of the active fragment and the function of DTT in the biological action, we investigated interactions of the peptide with vesicles resembling of the vesicle inversely dependenet on the cocenctration of DTT.
- 제목
- Characterization of the unique function of self aggregation and disulfide dimerization of the peptdie with membrane permeability
- 제목 (타언어)
- 지질막 투과성을 가지는 펩타이드의 자기 결합과 이중화의 독특한 특성 파악
- 저자
- LEE, KEUN HYEUNG
- 학회명
- 제7회 펩타이드 심포지엄