Executive Summary : | Phosphorylation of peptides is a crucial post-translational modification that controls various protein functions, including metabolism, transcription, cell cycle progression, apoptosis, and differentiation. A balance between kinases and phosphatases is essential for regulating these processes. This project aims to develop biocompatible fluorescent polymers that can detect trace-level phosphorylated biomolecules, such as peptides and proteins, via signal amplification. Metallosalen-based polymeric materials with linker units of different lengths will be synthesized, exposed to a wide range of phosphopeptides, and controlled experiments will ensure better response towards phosphopeptides. The selectivity of the polymeric materials towards phosphorylated proteins will be examined, including a wide range of Metallo- and non-metalloproteins and various phosphoproteins based on their degrees of phosphorylation. The newly designed Metallo (salen) polymers will be able to distinguish between poly- and monophosphorylated sites of the proteins. The superior binding ability of metallopolymers towards phosphopeptides will be exploited to monitor the activities of various protein kinase and phosphatase enzymes. After optimizing the sensing studies in the solution phase, paper-based color strips for phosphorylated peptide molecules will be developed, with the extent of fluorescence change proportional to the amount of phosphopeptides present in the sample. The sensory system will be employed for the estimation of casein protein in milk and other dairy products, with the presence of casein independently determined by a commercially available assay kit. |