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Effect of polymer chain density on protein-polymer conjugate conformation.

08:00 EDT 1st April 2019 | BioPortfolio

Summary of "Effect of polymer chain density on protein-polymer conjugate conformation."

Many biomedical applications employ covalent attachment to synthetic polymers to enhance the efficiency of proteins or other therapeutically active molecules. We report here the impact of polymer conjugation on the structural and thermal stability of a protein model, the bovine serum albumin, using a variable number of linear biodegradable polyphosphoesters, which were covalently tethered to the protein. We observed that BSAs' secondary structure measured by circular dichroism is independent of the conjugation. Small angle neutron scattering, however reveals a change from ellipsoid to globular shape of the whole complex arising from a slight compaction of the protein core and an increase of the polymer's radius of gyration as a function of the grafting polymer density. In particular, we highlight a gradual change of the polymer conformation around the protein and elongation of the semi-major dimension of the ellipsoidal protein. Our results will contribute to the description of biophysical characteristics of a new class of biologically relevant protein-polymer conjugates.

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This article was published in the following journal.

Name: Biomacromolecules
ISSN: 1526-4602
Pages:

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