Strategies for Reducing the Binding pH

As mentioned above, the binding pH of conventional boronate affinity in aqueous solution should be 8.5, which gives rise to not only the inconvenience of pH adjustment but also the risk of degradation of labile compounds since the pH of frequently used biosamples, such as blood, tear and saliva ranges from 4.5 to 8.0. To address this issue, novel boronic acids and innovative methods that allow for binding cis-diols in a real sample pH environment are in great demand. 

4KN-a]lylaulfimoyl)phcnylboronlc ecid a-wnino miTOphmyl)boKmic acid 

6-di4Mt -2,5-dia2a oxamyl)-pheiiyllMn nic acid 2,4-di flucrc-S -fcrmyl-phcnyIboronic acid 

The binding strength of common boronic acids toward ris-diol-contain-ing compounds is relatively weak, with dissociation constants (fif d) between boronic acids and sugars or glycoproteins ranging from 10 to 10  

capture of czs-diol-containing biomolecules, especially glycoproteins, of very low concentration by conventional boronate affinity materials is rather difficult or impossible. Therefore, it is essential to develop novel boronic acids ligands or boronate affinity materials that can significantly improve the binding strength. 

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