4.7 Article

Effect of poly(tert-butyl methacrylate) stereoregularity on polymer film interactions with peptides, proteins, and bacteria

Journal

COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 210, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.colsurfb.2021.112248

Keywords

Poly(tert-butylmethacrylate); Polymer tacticity; Protein adsorption; Bacterial adhesion

Funding

  1. National Science Centre of Poland [UMO-2016/21/D/ST5/01633]
  2. European Regional Development Fund [POIG.02.01.00-12-023/08]
  3. European Regional Development Fund Operational Program on Infrastructure and Environment [POIS 13.01.00-00-062/08]

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The study investigates the impact of polymer stereoregularity on its interactions with peptides, proteins, and bacteria strains, showing that different stereoregular forms of PtBMA affect the orientation and interactions with biomolecules differently. The stereoregularity influences the interactions with peptides, the orientation of immunoglobulin G, and the conformational changes in bovine serum albumin structure. Furthermore, Gram-positive bacteria (S. aureus) preferentially absorbed onto iso-PtBMA films compared to other stereoregularities.
The impact of polymer stereoregularity on its interactions with peptides, proteins and bacteria strains was studied for three stereoregular forms of poly(tert-butyl methacrylate) (PtBMA): isotactic (iso), atactic (at) and syndiotactic (syn) PtBMA. Principal component analysis of the time-of-flight secondary ion mass spectrometry data recorded for thin polymer films indicated a different orientation of ester groups, which in the case of isoPtBMA are exposed away from the surface whereas for at-PtBMA and syn-PtBMA these are located deeper within the film. This arrangement of chemical groups modified the interactions of iso-PtBMA with biomolecules when compared to at-PtBMA and syn-PtBMA. For peptides, the affected interactions were explained by the preferential hydrogen bonding and electrostatic interaction between the exposed polar ester groups of iso-PtBMA and positively charged peptides. In turn, for protein adsorption no impact on the amount of adsorbed proteins was observed. However, the polymer stereoregularity influenced the orientation of immunoglobulin G and induced conformational changes in bovine serum albumin structure. Moreover, the impact of polymer stereoregularity occurred equally for their interactions with Gram-positive bacteria (S. aureus), which absorbed preferentially onto iso-PtBMA films as compared to two other stereoregularities.

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