Brian F. Volkman, PhD
BS, Butler University, 1989
Dr. Volkman obtained his Bachelor of Science degree in Chemistry and Physics from Butler University in 1989 and his Doctorate degree from The University of California at Berkeley. The latter was awarded in 1994 for structural studies on proteins involved in bacterial gene regulation using NMR spectroscopy. Dr. Volkman's postdoctoral training was in the Department of Biochemistry at the University of Wisconsin-Madison. In 2000, Dr. Volkman started at the Medical College of Wisconsin where he is Professor in the Biochemistry Department. Dr. Volkman's work focuses on the structural biology of immunological signaling molecules and the use of NMR spectroscopy in structural proteomics.
- Amino Acid Sequence
- Binding Sites
- Chemokine CCL21
- Chemokine CXCL12
- Chemokines, C
- Chemokines, CXC
- Computational Biology
- Crystallography, X-Ray
- Drug Design
Our goal is to invent new ways to treat cancer and other ailments by examining the three-dimensional architecture of proteins involved in disease and synthesizing new drug candidate molecules. This research links the expertise of chemists, structural biologists, and clinician-scientists who collaborate in the design and testing of potential therapies. Graduate students in my group have invented and patented new compounds that show promise as treatments for cancer and psoriasis. Your donation helps us accelerate the drug development process by paying for preclinical studies that most research grants simply won’t support - bridging the gap between our basic science discoveries and clinical trials.
We use NMR spectroscopy and many other techniques to (1) understand the transmission of biological signals in terms of molecular structure, recognition and dynamics and (2) exploit this knowledge for the design and discovery of new molecules with practical utility as research tools, bioactive nanomaterials, or new drugs.
Dynamics and folding. Protein function is exquisitely dependent on compactly folded structures that combine energetic stability with intrinsic flexibility. Our work has revealed surprising new examples of conformational variability and altered the established paradigm for protein folding to include the new category of ‘metamorphic’ proteins. We are now trying to define the thermodynamic and evolutionary origins of metamorphic folding using the divergence of human lymphotactin from the rest of the chemokine family as a prototypical example. Other projects analyze novel modes of conformational switching that control cell polarity and enzyme activity.
Molecular recognition. Biological signals are often controlled by promoting or disrupting the interaction between two proteins. Many chemokines have been directly implicated in human diseases. Compounds that block chemokine signaling might function as inhibitors of inflammation, cancer progression, viral infection or autoimmune disease. We recently used NMR to solve the structure of the first chemokine-receptor complex, and subsequently used the details of this interface to search for small molecule ligands that bind the chemokine and block its activity. A hybrid in silico/NMR approach to inhibitor screening is now being used to target multiple chemokines with the ultimate goal of drug discovery to treat metastatic cancer and psoriasis.
Back Row L. to R.: Chris Veldkamp, Francis Peterson, Rob Tyler, Anthony Getschman (hands), Austin Jiang,
Alex Chadwick, Davin Jensen, Dustin Whitney and Josh Weiner
Middle Row L. to R.: Chad Koplinski, Amanda Nevins
First Row L. to R.: Dr. Brian Volkman, Echo the dog, Jamie Wieting, Becky Holme
(Beltrán J, Steiner PJ, Bedewitz M, Wei S, Peterson FC, Li Z, Hughes BE, Hartley Z, Robertson NR, Medina-Cucurella AV, Baumer ZT, Leonard AC, Park SY, Volkman BF, Nusinow DA, Zhong W, Wheeldon I, Cutler SR, Whitehead TA.) Nat Biotechnol. 2022 Jun 20 PMID: 35726092 06/22/2022
(Dishman AF, Volkman BF.) Curr Opin Struct Biol. 2022 Jun;74:102380 PMID: 35561475 SCOPUS ID: 2-s2.0-85129771683 05/14/2022
(Chi YI, Stodola TJ, de Assuncao TM, Volkman B, Smith B, Mathison AJ, Lomberk G, Zimmermann MT, Urrutia R.) FASEB J. 2022 May;36 Suppl 1 PMID: 35555661 SCOPUS ID: 2-s2.0-85130046941 05/14/2022
(Jorge SD, Chi YI, de Assuncao TM, Mathison AJ, Volkman B, Smith B, Lomberk G, Zimmermann MT, Urrutia R.) FASEB J. 2022 May;36 Suppl 1 PMID: 35553749 SCOPUS ID: 2-s2.0-85130006059 05/14/2022
(Powers HR, Jenjak SE, Volkman BF, Sahoo D.) FASEB J. 2022 May;36 Suppl 1 PMID: 35552332 SCOPUS ID: 2-s2.0-85130046210 05/14/2022
(Schlimgen R, Peterson F, Heukers R, Smit M, McCorvy J, Volkman B.) FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 1 May 2022;36 PMID: 35552343 SCOPUS ID: 2-s2.0-85130030169 05/01/2022
(Gupta P, Kadamberi IP, Mittal S, Tsaih SW, George J, Kumar S, Vijayan DK, Geethadevi A, Parashar D, Topchyan P, McAlarnen L, Volkman BF, Cui W, Zhang KYJ, Di Vizio D, Chaluvally-Raghavan P, Pradeep S.) Adv Sci (Weinh). 2022 05;9(14):e2104452 PMID: 35289120 PMCID: PMC9108620 SCOPUS ID: 2-s2.0-85126251446 03/16/2022
(Berg C, Wedemeyer MJ, Melynis M, Schlimgen RR, Hansen LH, Våbenø J, Peterson FC, Volkman BF, Rosenkilde MM, Lüttichau HR.) PLoS Pathog. 2022 03;18(3):e1010355 PMID: 35271688 PMCID: PMC8939814 SCOPUS ID: 2-s2.0-85127373696 03/11/2022
(Lewandowski EM, Kroeck KG, Jacobs LMC, Fenske TG, Witt RN, Hintz AM, Ramsden ER, Zhang X, Peterson F, Volkman BF, Veldkamp CT, Chen Y.) Biochemistry. 2022 03 01;61(5):311-318 PMID: 35156805 SCOPUS ID: 2-s2.0-85125310513 02/15/2022
(Brandum EP, Jørgensen AS, Calvo MB, Spiess K, Peterson FC, Yang Z, Volkman BF, Veldkamp CT, Rosenkilde MM, Goth CK, Hjortø GM.) Int J Mol Sci. 2022 Jan 26;23(3) PMID: 35163323 PMCID: PMC8836243 02/16/2022
(D'Uonnolo G, Reynders N, Meyrath M, Abboud D, Uchański T, Laeremans T, Volkman BF, Janji B, Hanson J, Szpakowska M, Chevigné A.) Front Immunol. 2022;13:868579 PMID: 35720349 PMCID: PMC9198273 06/21/2022
(Chi YI, Stodola TJ, De Assuncao TM, Leverence EN, Smith BC, Volkman BF, Mathison AJ, Lomberk G, Zimmermann MT, Urrutia R.) Comput Struct Biotechnol J. 2022;20:2200-2211 PMID: 35615018 PMCID: PMC9111933 SCOPUS ID: 2-s2.0-85130080827 05/27/2022