Dr. Amzel’s research focuses on structural mechanistic biochemistry and structural thermodynamics. Amzel was the first to uncover the structure of part of an antibody, the molecule that helps the human immune system fight off infection. He was also part of a team of researchers at Johns Hopkins who produced the first high-resolution pictures of how antibodies interact with antigens, foreign molecules invading the body.
Since then, Amzel has determined the structure of many proteins and protein complexes. Amzel also studies how proteins fold and take on their three-dimensional shapes and how proteins catalyze biochemical reactions within cells. Some of his findings are being used to design drugs targeting the enzymes.
Dr. Amzel’s lab is studying the catalytic mechanism of several enzyme families, using molecular biology, biochemistry and structural biology. They are studying both enzymes that recognize or process phosphates and redox enzymes. Cloning and expression, ultrapurification, kinetic characterization, mutational analysis, mass spectrometry, crystallization, and structure determination by x-ray diffraction are some of the techniques the lab uses to characterize the mechanisms of these enzymes. As the team uncovers information about the enzyme systems, other researchers are designing new drugs based on their discoveries.
In addition to enzyme studies, Dr. Amzel’s lab studies structural thermodynamics. Researchers in his lab have developed several systems, including anti-peptide antibodies and lectins, to see how proteins interact and bond to macromolecules or ligands. They are developing computational methods to calculate the changes in the thermodynamic variables that take place when a protein recognizes another macromolecule or a small ligand. As research in this lab reveals more about binding energetics, other researchers can take that knowledge and apply it to structure-based drug design.
Lab Website: Structural Enzymology and Thermodynamics Group
View all on PubMed
Aripirala S, Gonzalez-Pacanowska D, Oldfield E, Kaiser M, Amzel LM, Gabelli SB. “Structural and thermodynamic basis of the inhibition of Leishmania major farnesyl diphosphate synthase by nitrogen-containing bisphosphonates.” Acta Crystallogr D Biol Crystallogr. 2014 Mar
Phelps BR, Ahmed S, Amzel A, Diallo MO, Jacobs T, Kellerman SE, Kim MH, Sugandhi N, Tam M, Wilson-Jones M, Child Survival Working Group of the Interagency Task Team on the Prevention, Treatment of HIV infection in Pregnant Women, Mothers, Child. “Linkage, initiation and retention of children in the antiretroviral therapy cascade: an overview.” AIDS. 2013 Nov;27 Suppl 2:S207-13. doi: 10.1097/QAD.0000000000000095.
Sugandhi N, Rodrigues J, Kim M, Ahmed S, Amzel A, Tolle M, Dziuban EJ, Kellerman SE, Rivadeneira E; Child Survival Working Group of the Interagency Task Team on the Prevention and Treatment of HIV infection in Pregnant Women, Mothers and Children. “HIV-exposed infants: rethinking care for a lifelong condition.” AIDS. 2013 Nov;27 Suppl 2:S187-95. doi: 10.1097/QAD.0000000000000090.
Amzel A, Toska E, Lovich R, Widyono M, Patel T, Foti C, Dziuban EJ, Phelps BR, Sugandhi N, Mark D, Altschuler J; Child Survival Working Group of the Interagency Task Team on the Prevention and Treatment of HIV-infection in Pregnant Women, Mothers and Children. “Promoting a combination approach to paediatric HIV psychosocial support.” AIDS. 2013 Nov;27 Suppl 2:S147-57. doi: 10.1097/QAD.0000000000000098.
Bolduc D, Rahdar M, Tu-Sekine B, Sivakumaren SC, Raben D, Amzel LM, Devreotes P, Gabelli SB, Cole P. “Phosphorylation-mediated PTEN conformational closure and deactivation revealed with protein semisynthesis.” Elife. 2013 Jul 9;2:e00691. doi: 10.7554/eLife.00691.