The roles of phosphates in living organisms are vital and far-reaching, ranging from being structural components of DNA, RNA, and metabolites to facilitating biochemical processes through protein phosphorylation. Both over- and under-regulation of phosphates are indicative of many human diseases and disorders; therefore, the ability to monitor phosphate levels can greatly aid in the diagnosis and understanding of such conditions. Many biomolecules have been engineered to selectively recognize phosphates, including small molecules, proteins, antibodies, and peptides. On the other hand, peptides have been gaining increasing interest as a vehicle for drug delivery due to their ability to target protein-protein interactions with high affinity and selectivity, high cellular stability, and low cytotoxicity. Potent peptide binders for specific phosphate-containing targets can be screened from a peptide library, then those binders can be conjugated to fluorescent dyes to be used as sensors for such targets. In this research, a peptide inhibitor of pAkt2 was cyclized using different fluorescent dyes to find the optimal conditions to make a phosphate-sensing peptide that is both potent and easily sequenced. These conditions would be applied to make phosphate-sensing peptide libraries in the future.

Development of a phosphate-sensing cyclic peptide library

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.