Loading...
THE PREPARATION AND CHARACTERIZATION OF PRO-APOPTOTIC PEPTIDE ALA-VAL-PRO-ILE AND ITS DERIVATIVES
Fang, Shinong
Fang, Shinong
Citations
Altmetric:
Genre
Thesis/Dissertation
Date
2018
Advisor
Committee member
Group
Department
Bioengineering
Subject
Permanent link to this record
Collections
Research Projects
Organizational Units
Journal Issue
DOI
http://dx.doi.org/10.34944/dspace/2822
Abstract
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.
Description
Citation
Citation to related work
Has part
ADA compliance
For Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu