Abstract

Abstract IR spectroscopic conformational analyses of Boc–Glyn–OBzl (n=3–7) and Boc–(β-Ala)n–OBzl (n=3–8) were performed in the solid state, suggesting the occurrence of the β-sheet structure in the higher oligomers (n=5–8). Solubility data indicate that insolubilities of Boc–Glyn–OBzl and Boc–(β-Ala)n–OBzl in high-polar solvents begin at hexa- and heptapeptide levels, respectively. Insolubility of protected homooligopeptides of Gly and β-Ala was estimated to be caused by β-sheet aggregation. The high potential for the β-sheet formation of Boc–Glyn–OBzl and Boc–(β-Ala)n–OBzl (n≥5) could clearly be attributed to the great freedom of the peptide backbone dihedral angles of each of the Gly and β-Ala residues in the β-sheet structure. The implications of a replacement of a few Gly residues with β-Ala residues in surface regions of proteins are also discussed.

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