The easy disruption of the .BETA.-sheet structure of resin-bound human proinsulin C-peptide fragments by strong electron-donor solvents.
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概要
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The β-sheet structure disruption of cross-linked polystyrene resin-bound human proinsulin C-peptide fragments containing Pro residues at suitable intervals was investigated by a solvent titration method in CH<SUB>2</SUB>Cl<SUB>2</SUB>, mainly using TFE and HMPA as titrating solvents. The easy disruption of the β-sheet structure of resin-bound peptides in CH<SUB>2</SUB>Cl<SUB>2</SUB> by TFE and HMPA strongly suggested that the concept of "the peptide segment separation by tertiary peptide bonds" was useful for estimating the β-sheet-structure-disrupted behavior and that the β-sheet structure of the protected peptides having high 〈<I>P</I><SUB>c</SUB>〉 values could easily be disrupted in a medium electron-acceptor solvent of CH<SUB>2</SUB>Cl<SUB>2</SUB> by the addition of a strong electron-donor solvent of HMPA in spite of the electron donor-acceptor interaction between solvents. The present results indicate that effective solvents for solid-phase peptide synthesis by a fragment condensation procedure should be searched by taking the average helix, β-sheet, and coil conformation values, 〈<I>P</I><SUB>α</SUB>〉, 〈<I>P</I><SUB>β</SUB>〉, and 〈<I>P</I><SUB>c</SUB>〉, of peptide segments into consideration.
- 公益社団法人 日本化学会の論文
著者
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Narita Mitsuaki
Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A
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Yoshida Toshihiko
Department Of Applied Physics Faculty Of Engineering Osaka University
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Umeyama Hiroshi
Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology
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