• THE PREPARATION AND CHARACTERIZATION OF PRO-APOPTOTIC PEPTIDE ALA-VAL-PRO-ILE AND ITS DERIVATIVES

      Suh, Won H.; Lelkes, Peter I.; Pleshko, Nancy (Temple University. Libraries, 2018)
      The tetra-peptide sequence alanine-valine-proline-isoleucine (AVPI) is derived from a known inhibitor of apoptosis inhibitor proteins (IAPs) called Smac (second mitochondria-derived activator of caspases). Ala-Val-Pro-Ile can be further utilized as an anti-cancer agent by inhibiting the activities of apoptosis inhibitors so caspases can trigger apoptosis of cancer cells. AVPI, however, has poorly cell-penetration property thus limiting its ability to be utilized as a therapeutic agent for cancer treatments. We conjugated the AVPI molecule to a newly developed cell-penetrating peptide (CPP) called PepB to circumvent the situation of limited cellular availability. Solid Phase Peptide Synthesis (SPPS) methods have been utilized to prepared AVPI peptide derivatives. Key characterizations involve reverse-phase high-performance liquid chromatography (RP-HPLC), mass spectrometry, optical and fluorescence microscopy.