Peptide Synthesis for Potential Therapeutics

Peptides have a variety of applications, and are formed by linking two or more amino acids through peptide bonds. Peptides with certain amino acid sequences have shown anti-cancer activity. Our primary focus is to synthesize oligopeptides with different amino acid sequences. These peptides are carefully synthesized in precise sequences to ensure their efficacy. Additional studies will be carried out using complementary cell based experiments to understand the potential therapeutic effects that peptides may have. The solid phase peptide synthesis begins with rink amide resin, which serves as the structural foundation for the peptide. After filling a vessel with the rink amide resin, it undergoes an initial deprotection step using 20% piperidine in dimethylformamide (DMF), in order to remove the F-moc protecting group found in the resin. Once the protecting group is removed, the resin is washed with methanol (MeOH), Dichloromethane (DCM), and DMF, to further remove any unwanted reagents. The resin is then coupled with the appropriate amino acid. In the coupling process, DMF, Hexafluorophosphate Benzotriazole Tetramethyl Uronium (HBTU), and N,N'-Diisopropylethylamine (DIPEA) are mixed with the amino acids. Once synthesized, the peptide is cleaved from the resin and undergoes purification to remove any impurities. Finally, the peptide is lyophilized, which further isolates the desired product. The synthesized peptides were validated by mass spectrometry, confirming their identity and amino acid sequence.