Characterizing Novel Peptides as Anti-Thrombosis Agents
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The peptides in this study are based on two peptides in the literature that competitively bind collagen. The literature compounds would be degraded by the body’s enzymes due to the presence of the unstable disulfide bond therefore the peptides described here have this bond replaced with a head-to-tail method for cyclization, which would prevent ring opening. The third amino acid was changed to either 2,3 diaminopropionic acid (Dap) or threonine (Thr) to increase the compounds’ solubility in water. The literature compounds had IC50 values of 100 + 12.7 mM (N-peptide) and 34.8 + 8.59 mM (Q-peptide). The goal is to synthesize a head-to-tail cyclized peptide with an IC50 value less than or equal to the literature compounds with enhanced stability.
Department of Chemistry
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