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Impact of polypeptide sequence on thermal properties for diblock, random, and alternating copolymers containing a stoichiometric mixture of glycine and valine

This paper describes the experimental elucidation for the impact of polypeptide sequence on the solution structure and the thermo-responsivity, having considered the corresponding theoretical prediction using a binary pattern of hydrophobic and hydrophilic units. We prepare diblock, random, and alternating copolymers consisting of a stoichiometric amount of valine as a hydrophobic unit and glycine as a hydrophilic unit. Through the thermo-responsivity measurements of aqueous polymer solutions, it is found that the UV spectra of diblock copolypeptide exhibit a cloud point upon heating, which indicate that the polymer adopts a random coil structure at low temperature. On the other hand, the alternating peptide shows an upper critical solution temperature (UCST) behavior indicating a globule-to-coil transition upon heating. The opposite behavior of alternating peptide to that of diblock copolypeptide is found to be dependent on not the chirality of repeating units but the alternating binary pattern of hydrophobic and hydrophilic units. The random copolypeptide exhibits not only coil-to-globule transition at low temperature but also globule-to-coil transition at high temperature owing to the presence of both segregated and alternating polymer sequences in the polymer. The thermo-responsive structures of the polymers in an aqueous media are also discussed by determining the thermodynamic parameters for the transitions.

» Author: Abu Bin Ihsan, Yasuhito Koyama

» Reference: 10.1016/j.polymer.2018.12.021

» Publication Date: 17/12/2018

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