|| Gregg B. Fields
Robert A. Welch Foundation Distinguished University Professor in Chemistry
Office Phone: : (210) 567-1312
Office:542C.1 Medical School Building
University of Texas Health Science Center at San Antonio (UTHSCSA)
Department of Biochemistry
7703 Floyd Curl Drive
Areas of Specialization
• Solid-Phase Chemistry
• Extracellular Matrix Biochemistry
• Chemical Biology
My laboratory’s research interests are in the use of chemical approaches to better understand how protein three-dimensional structures influence cellular and enzymatic behaviors. Early studies included the systematic examination of mild methodologies for solid-phase synthesis of small proteins. Chemical approaches have been used to develop “mini-protein” models for the study of cellular recognition processes, which in turn allowed for the mapping of protein domains involved in tumor cell binding and signal transduction. Mini-protein models have subsequently been utilized to dissect the mechanisms of collagen catabolism, and in the process have provided new avenues for protease inhibitor design.
Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.
Lauer-Fields JL, Chalmers MJ, Busby SA, Minond D, Griffin PR, Fields GB.
J Biol Chem. 2009 Jul 1. [Epub ahead of print]
Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.
Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K, Fields GB
J Biol Chem. 2008 Jul 18;283(29):20087-95.
High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate.
Lauer-Fields JL, Minond D, Chase PS, Baillargeon PE, Saldanha SA, Stawikowska R, Hodder P, Fields GB.
Bioorg Med Chem. 2009 Feb 1;17(3):990-1005.
Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate.
Lauer-Fields JL, Spicer TP, Chase PS, Cudic M, Burstein GD, Nagase H, Hodder P, Fields GB.
Anal Biochem. 2008 Feb 1;373(1):43-51.
Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors.
Lauer-Fields J, Brew K, Whitehead JK, Li S, Hammer RP, Fields GB.
J Am Chem Soc. 2007 Aug 29;129(34):10408-17.
Synthesis and solid-phase application of suitably protected gamma-hydroxyvaline building blocks.
Cudic M, Marí F, Fields GB.
J Org Chem. 2007 Jul 20;72(15):5581-6.
Targeted drug delivery utilizing protein-like molecular architecture.
Rezler EM, Khan DR, Lauer-Fields J, Cudic M, Baronas-Lowell D, Fields GB.
J Am Chem Soc. 2007 Apr 25;129(16):4961-72.
Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences.
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Moss ML, Fields GB.
Biochemistry. 2007 Mar 27;46(12):3724-33.
. Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases
Lauer-Fields JL, Minond D, Sritharan T, Kashiwagi M, Nagase H, Fields GB..
J Biol Chem. 2007 Jan 5;282(1):142-50.
The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Visse R, Nagase H, Fields GB.
J Biol Chem. 2006 Dec 15;281(50):38302-13.