Polypeptides are building blocks in various natural proteins. Elastin is an important structural protein with an amino acid sequence valine-proline-glycine-valine-glycine (ValProGlyValGly) in its hydrophobic region. Due to its remarkable elasticity and stimuli-responsive properties, recently elastin and elastin-like polypeptides (ELPs) have been actively studied as biomaterials for various biomedical applications. Both proline and valine are key for such an elasticity. Chemoenzymatic polymerization of amino acids using proteases is eco-friendly, atom-economical method of polypeptide synthesis. In order to synthesize periodical amino acid sequence, the ValProGly-OEt and GlyProGly-OEt tripeptide ester were prepared as a monomer. These tripeptides were chemoenzymatically homopolymerized in phosphate buffer solution (1 M, pH 8.0) using papain at 40 oC for 2h. The tripeptides were also copolymerized with ValGly-OEt as a counterpart. All the obtained polypeptides were characterized by MALDI-TOF mass spectroscopy and 1H NMR spectrometry. The Circular dichroism (CD) spectra of poly(ValProGly-co-ValGly) revealed temperature dependent, reversible structural transition similar to that of tropoelastin (soluble precursor of elastin). Furthermore, post-polycondensation reaction of poly(ValProGly-co-ValGly) in the presence of polyphosphoric acid as a condensing agent at elevated temperature resulted in a higher molecular weight product, PP-poly(ValProGly-co-ValGly). PP-poly(ValProGly-co-ValGly) showed different secondary structure and thermal properties compared to poly(ValProGly-co-ValGly).

Synthesis of elastin mimicking polypeptide consisting of periodic di- and tri-peptide motifs by chemoenzymatic polymerization

256th National Meeting (2018)

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