Abstract
Abstract 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 CH2Cl2 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 CH2Cl2 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.
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