Kinetics of temperature response of PEO-b-PNIPAM-b-PAA triblock terpolymer aggregates and of their complexes with lysozyme

POLYMER

卷:83

Article

Papagiannopoulos, Aristeidis¹  Meristoudi, Anastasia¹  Hong, Kunlun²  Pispas, Stergios¹ 

[1] Natl Hellen Res Fdn, Inst Theoret & Phys Chem, GR-11635 Athens, Greece

[2] Oak Ridge Natl Lab, Ctr Nanophase Mat Sci, Oak Ridge, TN USA

关键词: Thermoresponsive polymers;    Protein complexation;    Kinetics;   

DOI  :  10.1016/j.polymer.2015.12.023

来源: Elsevier

【 摘 要 】

We present the kinetics of temperature response of a PEO-b-PNIPAM-b-PAA triblock terpolymer and of its complexes with lysozyme in aqueous solution. It is found that during the coil-to-globule transition of PNIPAM new bonds within the polymer aggregates are created, making the transition of the aggregates partially irreversible. This effect is also found for the protein loaded PEO-b-PNIPAM-b-PAA aggregates whereas in this case protein globules appear to enhance the formation of bonds, making the transition totally irreversible. The internal dynamics of both aggregates and complexes are frozen once the temperature is increased upon PINIPAM's LCST in water and remain so even when the temperature drops below LCST. We investigate the complexation kinetics of lysozyme and PEO-b-PNIPAM-b-PAA and observe that it occurs in two stages, one where protein globules adsorb on single pre-formed aggregates and one where protein globules cause inter-aggregate clustering. (C) 2015 Elsevier Ltd. All rights reserved.

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