Precise generation of selective surface-confined glycoprotein recognition sites
- Submitting institution
-
The Open University
- Unit of assessment
- 12 - Engineering
- Output identifier
- 1456850
- Type
- D - Journal article
- DOI
-
10.1021/acsabm.9b00289
- Title of journal
- ACS Applied Bio Materials
- Article number
- -
- First page
- 2617
- Volume
- 2
- Issue
- 6
- ISSN
- 2576-6422
- Open access status
- Compliant
- Month of publication
- May
- Year of publication
- 2019
- URL
-
-
- Supplementary information
-
-
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- No
- Number of additional authors
-
4
- Research group(s)
-
-
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- Glycoproteins are key players in a wide variety of disease processes and there is a need for high-affinity materials suitable for selective glycoprotein binding. Here we describe a method involving supramolecular templating and molecular imprinting which yields highly reproducible synthetic recognition sites on surfaces. Dissociation constants for target glycoproteins are in the low micromolar range, with minimal binding to non-target glycoproteins. The synthetic strategy also distinguishes between glycosylated and non-glycosylated forms of the same glycoprotein with >5-fold difference in binding affinity. These functional materials, exhibiting unprecedented recognition performance, open up a wealth of opportunities in the biotechnological and biomedical fields.
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -
