Drexel University - Comprehensive, integrated academics enhanced by co-operative education, technology, and research opportunities. | Drexel University
Drexel University
Search events. View events.

All Categories

Click for help in using calendar displays. Print the contents of the current screen.
Display Format: 
Event Details
Notify me if this event changes.Add this event to my personal calendar.
Go Back
Chemistry Winter Seminar
Start Date: 2/23/2023Start Time: 11:00 AM
End Date: 2/23/2023End Time: 12:30 PM

Event Description
Ross Wang, PhD
Department of Chemistry, Temple University
"Fluorine-Displacement Based Chemical Probes to Interrogate Protein-Protein Interactions"
Post-translational modifications (PTMs) modify existing proteins with additional chemical functionalities, resulting in the mediation of signaling events underlying various cellular processes.  The dysregulation of PTMs has been closely related to the onset and/or relapse of human diseases.  Yet, many PTM-related non-histone proteins and enzymes remain to be elucidated in terms of their identity, functions, and roles in cellular activities such as activation, proliferation, and migration, simply due to the lack of tools for characterization.2  Despite the development of bioorthogonal chemical reactions such as “click chemistry”, few research programs have explored protein labeling or tagging with reduced sterics.  Towards this end, my group has invented a steric-free bioorthogonal reaction (fluorine-thiol displacement (FTDR))1 and has developed a novel class of FTDR-based imaging and proteomics probes aimed at a complete dissection of substrate proteins of acetylation that are featured in diseased cells such as cancer cell lines; which for now cannot be systematically profiled due to limitations in the current chemical proteomics approach that heavily relies on sterically hindered ‘click chemistry’ tags.1  
Concurrently, to facilitate the studying and targeting of any new protein-protein interactions (PPIs) to be revealed by the aforementioned research investigations in PTM signaling, we also exploited other tool probes3-4 such as peptide stapling4 based on the FTDR reaction.  The resulting peptides possessed improved folding, stability, and on-target affinity, but also displayed enhanced cell penetration than the peptides stapled by traditionally used ring-closing metathesis.4  As an on-going effort, my group has been applying this new class of peptides to interrogate Axin-β-catenin interactions and p53-MDM2 interactions that are key to the onset and relapse of breast cancers, leukemia, and lymphoma, etc, as well as PPIs of protein tyrosine phosphatases that are important to neuron regeneration.

Join us in person or on Zoom
Meeting ID: 919 2884 3726
Passcode: 243750
Contact Information:
Name: Myungwoon Lee
Phone: 215-895-1699
Email: ml3784@drexel.edu
Drexel University
Disque Hall 109
  • Undergraduate Students
  • Graduate Students
  • Faculty
  • Staff

  • Display Month:

    Advanced Search (New Search)
    Date Range:
    Time Range:

    Special Features: 

    Select item(s) to Search

    Select item(s) to Search
    Select item(s) to Search
    Select item(s) to Search