Chemoenzymatic Synthesis of Poly(l-alanine) in Aqueous Environment

l-Alanine ethyl ester was polymerized into poly­(l-alanine) (polyAla), one of the insoluble polypeptides, by papain in aqueous buffer at varying pH. At neutral pH, a maximum chain length of 11 repeats was observed. These polymers were dominated by random coiled structure and demonstrated a lack of p...

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Bibliographic Details
Published in:Biomacromolecules 2012-04, Vol.13 (4), p.947-951
Main Authors: Baker, Peter James, Numata, Keiji
Format: Article
Language:English
Subjects:
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Molecular Structure
Papain - chemistry
Papain - metabolism
Peptides - chemical synthesis
Peptides - metabolism
Water - chemistry
Water - metabolism
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Summary:l-Alanine ethyl ester was polymerized into poly­(l-alanine) (polyAla), one of the insoluble polypeptides, by papain in aqueous buffer at varying pH. At neutral pH, a maximum chain length of 11 repeats was observed. These polymers were dominated by random coiled structure and demonstrated a lack of patterned macromolecular assembly. Under alkaline conditions, longer polymer chain lengths were achieved, and the maximum chain length was 16 repeats. These longer chains showed distinct β-sheet formation and were capable of fibril assembly. The present study reports on chemoenzymatic synthesis of a hydrophobic homopolypeptide under aqueous conditions as well as demonstrates a chain length dependency of secondary structure formation and macromolecular assembly of chemoenzymatically synthesized polyAla, providing a new insight into material design of polypeptide.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm201862z