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Journal of Bioactive and Compatible Polymers
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The Synthesis and Properties of Block-Copoly(amino acid)s with Folded Structures: A Primitive Enzyme Model

Yasuo Suda

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Yasuhiro Ohe

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Yoshiko Okazaki

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Katsutoshi Tanimura

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Tadahiro Tetsumi

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Masatoshi Nishi

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

Masao Sumi

Faculty of Pharmaceutical Sciences Setsunan University 45-1, Nagaotouge-chou Hirakata, Osaka, Japan 573-01

As a model of a primitive enzyme block-copoly(amino acid)s con taining L-serine and L-aspartic acid as the repeat unit were prepared. Spectro scopic measurements indicate that some block-copoly(amino acid)s, especially ABAB and ABABA types, do form folded conformations. Hydrolysis reactions of p-nitrophenyl p-guanidinobenzoate were accelerated in the presence of ABAB and ABABA type block-copoly(amino acid)s compared with a random copoly (amino acid). From these results we speculate that primitive enzymes were born by assembling block-copoly(amino acid)s.

Journal of Bioactive and Compatible Polymers, Vol. 4, No. 2, 137-150 (1989)
DOI: 10.1177/088391158900400204
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