Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites

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Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites. / Mitchell, Philippa; Tommasone, Stefano; Angioletti-Uberti, Stefano; Bowen, James; Mendes, Paula M.

In: ACS Applied Bio Materials, Vol. 2, No. 6, 17.06.2019, p. 2617-2623.

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Mitchell, Philippa ; Tommasone, Stefano ; Angioletti-Uberti, Stefano ; Bowen, James ; Mendes, Paula M. / Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites. In: ACS Applied Bio Materials. 2019 ; Vol. 2, No. 6. pp. 2617-2623.

Bibtex

@article{c308ad19ad4b49328a5e63d55fd04ee0,
title = "Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites",
abstract = "Since glycoproteins have become increasingly recognized as key players in a wide variety of disease processes, there is an increasing need for advanced affinity materials for highly selective glycoprotein binding. Herein, for the first time, a surface-initiated controlled radical polymerization is integrated with supramolecular templating and molecular imprinting to yield highly reproducible synthetic recognition sites on surfaces with dissociation constants (KD) in the low micromolar range for target glycoproteins and minimal binding to nontarget glycoproteins. Importantly, it is shown that the synthetic strategy has a remarkable ability to distinguish the glycosylated and nonglycosylated forms of the same glycoprotein, with a >5-fold difference in binding affinity. The precise control over the polymer film thickness and positioning of multiple carbohydrate receptors plays a crucial role in achieving an enhanced affinity and selectivity. The generated functional materials of unprecedented glycoprotein recognition performance open up a wealth of opportunities in the biotechnological and biomedical fields.",
author = "Philippa Mitchell and Stefano Tommasone and Stefano Angioletti-Uberti and James Bowen and Mendes, {Paula M}",
year = "2019",
month = jun,
day = "17",
doi = "10.1021/acsabm.9b00289",
language = "English",
volume = "2",
pages = "2617--2623",
journal = "ACS Applied Bio Materials",
issn = "2576-6422",
publisher = "American Chemical Society",
number = "6",

}

RIS

TY - JOUR

T1 - Precise Generation of Selective Surface-Confined Glycoprotein Recognition Sites

AU - Mitchell, Philippa

AU - Tommasone, Stefano

AU - Angioletti-Uberti, Stefano

AU - Bowen, James

AU - Mendes, Paula M

PY - 2019/6/17

Y1 - 2019/6/17

N2 - Since glycoproteins have become increasingly recognized as key players in a wide variety of disease processes, there is an increasing need for advanced affinity materials for highly selective glycoprotein binding. Herein, for the first time, a surface-initiated controlled radical polymerization is integrated with supramolecular templating and molecular imprinting to yield highly reproducible synthetic recognition sites on surfaces with dissociation constants (KD) in the low micromolar range for target glycoproteins and minimal binding to nontarget glycoproteins. Importantly, it is shown that the synthetic strategy has a remarkable ability to distinguish the glycosylated and nonglycosylated forms of the same glycoprotein, with a >5-fold difference in binding affinity. The precise control over the polymer film thickness and positioning of multiple carbohydrate receptors plays a crucial role in achieving an enhanced affinity and selectivity. The generated functional materials of unprecedented glycoprotein recognition performance open up a wealth of opportunities in the biotechnological and biomedical fields.

AB - Since glycoproteins have become increasingly recognized as key players in a wide variety of disease processes, there is an increasing need for advanced affinity materials for highly selective glycoprotein binding. Herein, for the first time, a surface-initiated controlled radical polymerization is integrated with supramolecular templating and molecular imprinting to yield highly reproducible synthetic recognition sites on surfaces with dissociation constants (KD) in the low micromolar range for target glycoproteins and minimal binding to nontarget glycoproteins. Importantly, it is shown that the synthetic strategy has a remarkable ability to distinguish the glycosylated and nonglycosylated forms of the same glycoprotein, with a >5-fold difference in binding affinity. The precise control over the polymer film thickness and positioning of multiple carbohydrate receptors plays a crucial role in achieving an enhanced affinity and selectivity. The generated functional materials of unprecedented glycoprotein recognition performance open up a wealth of opportunities in the biotechnological and biomedical fields.

U2 - 10.1021/acsabm.9b00289

DO - 10.1021/acsabm.9b00289

M3 - Article

C2 - 31259319

VL - 2

SP - 2617

EP - 2623

JO - ACS Applied Bio Materials

JF - ACS Applied Bio Materials

SN - 2576-6422

IS - 6

ER -