Preparation of Boronate Affinity - Functionalized Metal-Organic Framework Material For Selective Recognition And Separation of Glycoprotein Under Physiological pH

Abstract

Glycoproteins play an important role in biological processes such as protein folding, information transmission, nerve conduction, and molecular recognition. Therefore, it is of great significance to design and develop an adsorbent with high adsorption capacity for glycoprotein. In this paper, a novel boronate affinity material (Zr-MOF@S-S@B) was prepared by combining Zr-MOF, disulfide covalent bond (-S-S-), 4-mercaptophenylboronic acid (4-MPBA) for selective enrichment of glycoprotein and elution of glycoprotein at physiological pH. The affinity between boric acid and cis - diol makes the composite material has a high adsorption capacity of 625.5 mg g -1 for ovalbumin (OVA). At the same time, the Zr-MOF@S-S@B has exhibited great reusability and large specific surface area. Furthermore, the material contains disulfide bonds that can release surface binding glycoprotein specifically under physiological pH conditions, effectively avoiding the reduction of glycoprotein activity. In general, the method is successfully used for the enrichment of OVA in egg white samples, which has broad application prospects in the study of glycoprotein.