Periodic introduction of aromatic units in polypeptides via chemoenzymatic polymerization to yield specific secondary structures with high thermal stability

November 13, 2019

Title

Periodic introduction of aromatic units in polypeptides via chemoenzymatic polymerization to yield specific secondary structures with high thermal stability

Author

Kousuke Tsuchiya, Naruki Kurokawa, Joan Gimenez-Dejoz, Prashant G. Gudeangadi, Hiroyasu Masunaga, Keiji Numata

Year

2019

Journal

Polymer Journal

Abstract

Polypeptides containing periodic aromatic residues in their main chains were synthesized via papain-catalyzed chemoenzymatic polymerization of tripeptide ester monomers under moderate conditions in aqueous buffers. As the monomer, 4-aminobenzoic acid (Abz) was modified with Gly or Ala at the N- and C-termini to mitigate the poor substrate specificity of papain to unnatural amino acids. The tripeptide esters, namely, GlyAbzGly and AlaAbzAla ethyl esters, can be recognized and polymerized by papain, resulting in the polypeptides poly(GlyAbzGly) and poly(AlaAbzAla), respectively, with periodic sequences containing Abz units every three residues. Copolymerization of tripeptide esters with Gly or Ala ethyl ester also proceeded in the presence of papain. The secondary structures of the Abz-containing polypeptides were investigated by IR and wide-angle X-ray diffraction (WAXD) analysis. The WAXD profile of poly(GlyAbzGly) was similar to that of polyGly, whereas poly(AlaAbzAla) adopted a sheet-like structure similar to the β-sheet of polyAla. Thermal analysis of Abz-containing polypeptides revealed that the high thermal stability of the Abz-containing polypeptides is related to the distinct sequences that periodically include Abz residues.

Instrument

J-820

Keywords

Circular dichroism, Secondary structure, Polymers, Biochemistry