Peptide medications, known for their high target specificity, safety, and adaptability, are well-suited to tackle modern biomedical challenges. Recent advancements in chemical modification and drug delivery have transformed peptide drugs into effective treatments for immune modulation, metabolic disorders, cancer, and resistant infections. Several FDA-approved peptides, such as icatibant, trofinetide, and rezafungin, utilize pyrrolidine (proline-derived) aza-heterocycles for receptor binding and structural stability. Additionally, aza-peptides like goserelin and atazanavir incorporate nitrogen in place of α-carbons to enhance metabolic stability and therapeutic efficacy. Moreover, the indole aza-heterocycle found in tryptophan is employed in FDA-approved peptide medications that include tryptophan to promote receptor selectivity, structural stability, and pharmacological effectiveness. These include GnRH agonists (such as leuprolide and goserelin), vasopressin analogs (like desmopressin), and somatostatin analogs (including octreotide and lanreotide). Aza-heterocycles undergo various organic transformations, including skeletal rearrangements, functionalization, and cycloaddition with electrochemically generated radical cation or radical anion intermediates. Our primary focus is the electrochemical modification of proline and tryptophan-specific peptides. We aim to modify the proline and tryptophan-containing peptide and evaluate their biological activity (anti-viral and anti-cancer) with our biological partners that respond to current therapeutic challenges.