Szczegóły publikacji
Opis bibliograficzny
Effect of poly(tert-butyl methacrylate) stereoregularity on polymer film interactions with peptides, proteins, and bacteria / Natalia Janiszewska, Joanna Raczkowska, Karolina Grzegorczyk, Monika Brzychczy-Włoch, Tomasz Gosiewski, Mateusz M. MARZEC, Katarzyna Gajos, Kamil Awsiuk // Colloids and Surfaces. B, Biointerfaces ; ISSN 0927-7765. — 2022 — vol. 210 art. no. 112248, s. 1–10. — Bibliogr. s. 9–10, Abstr. — Publikacja dostępna online od: 2021-11-26
Autorzy (8)
- Janiszewska Natalia
- Raczkowska Joanna
- Grzegorczyk Karolina
- Brzychczy-Włoch Monika
- Gosiewski Tomasz
- AGHMarzec Mateusz M.
- Gajos Katarzyna
- Awsiuk Kamil
Słowa kluczowe
Dane bibliometryczne
| ID BaDAP | 138023 |
|---|---|
| Data dodania do BaDAP | 2021-12-07 |
| Tekst źródłowy | URL |
| DOI | 10.1016/j.colsurfb.2021.112248 |
| Rok publikacji | 2022 |
| Typ publikacji | artykuł w czasopiśmie |
| Otwarty dostęp |  |
| Creative Commons | |
| Czasopismo/seria | Colloids and Surfaces, B, Biointerfaces |
Abstract
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 iso-PtBMA 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.
