Discrimination and highly selective adsorption of phosphoproteins and glycoproteins with arginine-functionalized polyhedral oligomeric silsesquioxane frameworks

The crosstalk between phosphoproteins and glycoproteins causes many difficulties in their selective isolation/enrichment from biological samples. This issue is of high significance in proteomics study, but thus far, it has not received proper attention. Herein, an arginine-functionalized polyhedral oligomeric silsesquioxane (POSS) framework, PP-x-Arg (x = 0, 1, 2, … denotes the amount of salt in preparation), was developed by combining salt-templated thermal polymerization of POSS and pyromellitic dianhydride (PMDA) with post-modification using arginine. PP-x-Arg possesses a porous nanostructure and abundant functional groups, namely, guanidine and zwitterionic groups, enabling the selective adsorption of phosphoproteins or glycoproteins via specific phosphate–guanidine affinity or hydrophilic interaction between PP-x-Arg and glycoproteins, respectively. In particular, the adsorption selectivity exhibited by PP-x-Arg can be easily regulated by adjusting the pH values of the adsorption medium. The PP-x-Arg framework was further employed for the discrimination and isolation of phosphoproteins and glycoproteins from biological samples.