| Budget Amount *help |
¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1986: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Research Abstract |
High molecular weight synthetic polypeptides have become the moldel for the general study of physical, chemical, and biological properties of proteins. A wide variety of peptide synthesis have been proposed. They are classified as the stepwise and repeating formation of a peptide bond or the condensation polymerization of amino acid derivatives. The former involves many unit process, so the yield of pure resulting peptide is remarkably decreased increasing amino acid residues in the peptide, because all unit process contain incomplet yield. The later is obtainable high molecular weight polypeptides in good yield. However, it is difficult to control exactly the amino acid sequences in the polypeptides.
It has been considered that anciently of all various amino acids existing in the sea were associated in various order and were reacted each other with catalitic dehydration by sun light or metalic ion to give various proteins. We considered as follows. When amino acid derivertives, i.e., several N-carboxy amino acid anhydrides, associate and polymerize each to each in a organic solvent, a polypeptide containing several amino acid residues in order, which relate to be a natural occurring protein, would be produced. We polymerize multicomponent of N-carboxy amino acid anhydrides to synthesize polypeptides with the semiregular sequence of amino acid residues, near natural proteins. The polypeptides formed were soluble in the polymerization solvent dichloroethane and able to cast films with high strenght and transparency. Optical rotatory dispersion of the copolypeptides in the solution show the pattern due to the helix or coiled conformation.
Copolymerization of tryptophan NCA with various NCA was carried out. The solubility was in some case sharply triptophan residue dependent.
The influence of conformation and configuration, especially of the phenyl pendant group, on the solubility of the copolypeptides in the aprotic solvents was discussed.
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