Design of the synthetic route for helical peptides. Synthesis and solubility of model peptides having a helical structure.

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概要

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• Fragment condensations between amino- and carboxyl-components of hydrophobic decapeptides, which have a β-sheet structure in the solid state and are insoluble in DMF, NMP, and DMSO, were examined in a mixture of CH<SUB>2</SUB>Cl<SUB>2</SUB> and TFE (4/1, v/v) using various coupling reagents. By the use of DCC and HOBt as coupling reagents, the reaction proceeded smoothly in moderate yield to give eicosapeptides. These have a stable helical structure in the solid state and are easily soluble in a variety of organic solvents. The hydrophobic eicosapeptides obtained were subjected to a successive coupling reaction in CH<SUB>2</SUB>Cl<SUB>2</SUB> alone to give helical tetracontapeptides in high yield, which also have high solubility in various organic solvents of low polarity. The solubility of hydrophobic helical peptides presents a solubility feature of helical peptides which are obtained as peptide intermediates in protein synthesis. The synthetic strategy for helical peptides and proteins is discussed in connection with the solubility prediction method.

• 公益社団法人 日本化学会の論文

著者

• Narita Mitsuaki

  Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A

• KOJIMA Yoshihisa

  Department of Molecular Pathology, Osaka University Graduate School of Medicine and Health Science

• Isokawa Shizuko

  Department of Industrial Chemistry, Faculty of Technology, Tokyo University of Agriculture and Technology

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