Our Group

We are a Chemical Biology group in the Department of Chemistry at Texas A&M University led by Assistant Professor Wenshe Liu. Our interest lies in utilizing organic Chemistry tools to decipher biological systems.

We are involved in the following major areas:

  • Organic Chemistry
  • Molecular Biology
  • Protein Evolution
  • Cell Biology

Please visit our Group Members page to learn more about our individual group members.

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Our Research

Using the genetic code expansion technique, a powerful tool to functionalize proteins, the genetically encoded amino acid inventory has been augmented far beyond the canonical 20 to include non-canonical amino acids that contain diverse chemical functional groups. This opens a door for an array of novel protein research.

Our major focus is to devise new genetic code expansion methods for the encoding of non-canonical amino acids in proteins in living cells and apply these methods in four major areas:

  1. Deciphering cancer epigenetics regulation of histone and P53
  2. Drug discovery using phase display
  3. Protein biosensor development for small molecular sensing and
  4. Development of new click chemical reporters for specific protein tagging and fluorescent cell imaging

Please visit our Publications page to see our latest work or visit Research to view the highlights of the research areas.

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Bioorthogonal Reactions for Protein Modifications

Bioorthogonal reactions refer to chemical reactions that were performed in a biological system without interfering with the complex cell environment. We use these reactions to develop potential click chemistry.

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Epigenetics

Understanding the genetic transcriptional control in biological systems allows us to provide a profound understanding of cancer biology and genetic disorders and may inspire new therapeutic methods to cure these diseases.

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Phage Display

Development of phage display and its methods will make it possible to target essential components and pathways within many different diseases, including cancer, AIDS, cardiovascular disease, and autoimmune disorders.

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Protein FRET labeling for biosensor development

Förster resonance energy transfer (FRET) between a pair of donor and acceptor dyes is an invaluable tool to study dynamic protein conformational changes such as conformation rearrangement and folding/unfolding.

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Group News

Dr. Wenshe Liu was interviewed by the ACS Chemical Biology editor for the issue highlight article “Genetic Incorporation of Twelve meta-Substituted Phenylalanine Derivatives Using a Single Pyrrolysyl-tRNA Synthetase Mutant”. Reference: ACS Chem. Biol., 2013, 8, 405-415. ARTICLE LINK/ INTERVIEW AUDIO LINK(Click on "February 2013")

"Contributors to the Emerging Invesitgators Issue: Wenshe Liu Profile" Mol. BioSyst. 2010; 6, 1526-1531 ARTICLE LINK

"Expanded Blueprint--Genetic incorporation of two different noncanonic amino acids into one protein" Angew. Chem. Int. Ed. 2010; 49, 3211-3214 PRESS LINK

"A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli" Angew. Chem. Int. Ed. has been selected as a hot paper by the journal editor.

"A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli" has been accepted by Angew. Chem. Int. Ed.