Protein Adsorption on Grafted Zwitterionic Polymers Depends on Chain Density and Molecular Weight. (2nd June 2020)
- Record Type:
- Journal Article
- Title:
- Protein Adsorption on Grafted Zwitterionic Polymers Depends on Chain Density and Molecular Weight. (2nd June 2020)
- Main Title:
- Protein Adsorption on Grafted Zwitterionic Polymers Depends on Chain Density and Molecular Weight
- Authors:
- Ahmed, Syeda Tajin
Leckband, Deborah E. - Abstract:
- Abstract: This study demonstrates that protein adsorption on end‐grafted, zwitterionic poly(sulfobetaine) (pSBMA) thin films depends on the grafting density, molecular weight, and ionic strength. Zwitterionic polymers exhibit ultralow nonspecific fouling (protein adsorption) and excellent biocompatibility. This picture contrasts with a recent report that soluble pSBMA chains bind proteins and alter the protein folding stability. To address this apparent contradiction, the dependence of protein adsorption on the chain grafting parameters is investigated: namely, the grafting density, molecular weight, and ionic strength. Studies compared the adsorption of phosphoglycerate kinase and positively charged lysozyme versus the scaled grafting parameter s /2 R F, where s is the distance between grafting sites and R F is the Flory radius. Plots of the adsorbed protein amount versus s /2 R F exhibit a bell‐shaped curve, with a maximum near s /2 R F ≈ 1 and an amplitude that decreases with ionic strength. This behavior is qualitatively consistent with theoretical models for colloid interactions with weakly attractive, grafted chains. The results confirm that proteins do adsorb to pSBMA thin films, and they suggest an underlying mechanism. Comparisons with polymer models further identify design rules for pSBMA films that effectively repel protein. Abstract : Protein adsorption on end‐grafted, zwitterionic poly(sulfobetaine) thin films depends on grafting density, molecular weight, andAbstract: This study demonstrates that protein adsorption on end‐grafted, zwitterionic poly(sulfobetaine) (pSBMA) thin films depends on the grafting density, molecular weight, and ionic strength. Zwitterionic polymers exhibit ultralow nonspecific fouling (protein adsorption) and excellent biocompatibility. This picture contrasts with a recent report that soluble pSBMA chains bind proteins and alter the protein folding stability. To address this apparent contradiction, the dependence of protein adsorption on the chain grafting parameters is investigated: namely, the grafting density, molecular weight, and ionic strength. Studies compared the adsorption of phosphoglycerate kinase and positively charged lysozyme versus the scaled grafting parameter s /2 R F, where s is the distance between grafting sites and R F is the Flory radius. Plots of the adsorbed protein amount versus s /2 R F exhibit a bell‐shaped curve, with a maximum near s /2 R F ≈ 1 and an amplitude that decreases with ionic strength. This behavior is qualitatively consistent with theoretical models for colloid interactions with weakly attractive, grafted chains. The results confirm that proteins do adsorb to pSBMA thin films, and they suggest an underlying mechanism. Comparisons with polymer models further identify design rules for pSBMA films that effectively repel protein. Abstract : Protein adsorption on end‐grafted, zwitterionic poly(sulfobetaine) thin films depends on grafting density, molecular weight, and ionic strength. This behavior is qualitatively consistent with theoretical models for colloid interactions with weakly attractive, grafted chains. … (more)
- Is Part Of:
- Advanced functional materials. Volume 30:Number 30(2020)
- Journal:
- Advanced functional materials
- Issue:
- Volume 30:Number 30(2020)
- Issue Display:
- Volume 30, Issue 30 (2020)
- Year:
- 2020
- Volume:
- 30
- Issue:
- 30
- Issue Sort Value:
- 2020-0030-0030-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2020-06-02
- Subjects:
- fouling -- grafting density -- polymer brushes -- protein adsorption -- zwitterionic polymer
Materials -- Periodicals
Chemical vapor deposition -- Periodicals
620.11 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1616-3028 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/adfm.202000757 ↗
- Languages:
- English
- ISSNs:
- 1616-301X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0696.853900
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 13679.xml