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Assessment of Glycoprotein Interactions With 4-[(2-aminoethyl)carbamoyl]phenylboronic Acid Surfaces Using Surface Plasmon Resonance Spectroscopy

Assessment of Glycoprotein Interactions With 4-[(2-aminoethyl)carbamoyl]phenylboronic Acid Surfaces Using Surface Plasmon Resonance Spectroscopy

Jennifer Macalindong De Guzman, Steven A Soper, Robin L McCarley

Anal Chem. 2010 Nov 1;82(21):8970-7.

PMID: 20919681

Abstract:

Reported here are analyses of the interactions between a select group of solution-phase glycoproteins and a unique boronic acid capture surface. The boronic acid derivative, 4-[(2-aminoethyl)carbamoyl]phenylboronic acid, AECPBA, was synthesized and then immobilized on carboxymethyl dextran surfaces using simple coupling methods. From surface plasmon resonance spectroscopy responses, it is found that model glycoproteins interact strongly with the AECPBA surface and subsequently can be readily released from the AECPBA surface using borate buffer. A striking difference between the glycoproteins fetuin and asialofetuin (desialylated fetuin), in terms of glycoprotein binding to the AECPBA surface, indicates that the interaction of glycoproteins with the immobilized AECPBA is dictated by the terminal saccharide of the heteroglycan chain. Surprisingly, secondary interactions of glycosylated and nonglycosylated proteins with the carboxymethyl dextran hydrogel matrix are observed. Importantly, it is demonstrated that use of tris(hydroxymethyl)aminomethane buffer allows for decreased secondary interactions of nonglycosylated proteins on the AECPBA/dextran surface, as noted with the model protein ExtrAvidin.

Chemicals Related in the Paper:

Catalog Number	Product Name	CAS Number	Price
AP159896158	4-(trans-2-Carboxyvinyl)phenylboronic acid	159896-15-8	Price
LS793645	(4-benzyloxy-2-formyl)phenylboronic acid		Price
LS793937	2-(Hydroxymethyl)phenylboronic acid		Price

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