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Issue 28, 2017
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Tuning the solution organization of cationic polymers through interactions with bovine serum albumin

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Abstract

The interactions of bovine serum albumin (BSA) with aggregates of cationic polymers, i.e. quaternized poly(chloromethyl styrene) chains (QIm-PCMS), in aqueous solutions are investigated using small angle neutron scattering on length scales relevant to the size of BSA. The arrangement of the macromolecular chains within their aggregates is consistent with a blob description of overlapping chains that contain hydrophobic domains. The local conformations depend on the salt content as in typical linear polyelectrolytes. Although the hydrophobic content of the cationic polymers does not cause measurable local morphology differences, the interactions with BSA are enhanced in the case of the not fully quaternized polymer. The secondary structure of BSA is critically compromised by the interaction with the quaternized polymers as the signature of the alpha helix conformation is lost. The complexation with BSA and the resulting enhancement of interchain associations on higher length scales are verified using dynamic light scattering experiments. This study demonstrates the ability to tune the polyelectrolyte/protein interactions and polyelectrolyte chain–chain associations by modifying the hydrophobic content of the polyelectrolytes.

Graphical abstract: Tuning the solution organization of cationic polymers through interactions with bovine serum albumin

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Publication details

The article was received on 25 Apr 2017, accepted on 20 Jun 2017 and first published on 20 Jun 2017


Article type: Paper
DOI: 10.1039/C7CP02704D
Citation: Phys. Chem. Chem. Phys., 2017,19, 18471-18480
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    Tuning the solution organization of cationic polymers through interactions with bovine serum albumin

    A. Papagiannopoulos, E. Vlassi, S. Pispas and C. J. Jafta, Phys. Chem. Chem. Phys., 2017, 19, 18471
    DOI: 10.1039/C7CP02704D

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