Protein-boronic acid conjugates and their binding to low-molecular-mass cis-diols and glycated hemoglobin.
Different methods for covalent linkage of phenylboronic acid (PBA) to structural proteins and enzymes are presented. Protein-PBA conjugates, free in solution or immobilised on magnetizable polymer particles, were tested for their binding of D-sorbitol, D-mannose and glycohemoglobin (GHb). Similarly, alkaline phosphatase-PBA conjugates were used in an attempted enzyme-linked sorbent assay for the detection of GHb. Affinity chromatography on immobilised D-mannose and gel chromatographic studies of protein-PBA complexes with [14C]sorbitol, clearly illustrated a low affinity of the interaction studied. Glycated hemoglobin could not be detected using the enzyme-linked sorbent assay approach. However, GHb was found to be specifically retained on columns filled with protein-PBA-coated particles as affinity matrix, enabling the glycation level of blood samples to be determined.
D001897:Boronic Acids / Q000378:metabolism*; D006442:Glycated Hemoglobin / Q000378:metabolism*; D008970:Molecular Weight; D011485:Protein Binding
D001897:Boronic Acids; D006442:Glycated Hemoglobin; C010686:benzeneboronic acid