Our research focus is on protein folding, structure and stability. It includes the analysis of the energetic-structure-function relationship and folding pathways in proteins and peptides by circular dichroism spectroscopy, differential scanning calorimetry, fluorescence, x-ray crystallography, and site-directed mutagenesis.
Our on-going NIH-funded work is aimed at understanding the energetic and structural basis for the conformational plasticity of apolipoproteins. These are protein constituents of lipoproteins that mediate lipid transport and metabolism and are central in the pathogenesis of atherosclerosis, stroke, and certain forms of amyloidosis. Apolipoproteins are distinct in their structural adaptability to various lipoprotein particles and to plasma. We try to understand in molecular detail the energetic and structural basis for this adaptability.
A major focus of our research is on the molecular mechanisms of lipoprotein stabilization and fusion. In 2002 we revealed that lipoprotein stability is determined by kinetic barriers. Similar barriers may modulate in-vivo lipoprotein transformations. Our goal is to obtain key molecular determinants for these energy barriers.
- Graduate Faculty (Primary Mentor of Grad Students), Boston University School of Medicine, Graduate Medical Sciences
- Brandeis University, PhD
- Moscow State University, MS
- Published on 9/19/2018
Morgado I, Panahi A, Burwash AG, Das M, Straub JE, Gursky O. Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation. Biochemistry. 2018 Oct 02; 57(39):5738-5747. PMID: 30184436.
- Published on 7/13/2018
Wilson CJ, Das M, Jayaraman S, Gursky O, Engen JR. Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A-I in Model Lipoproteins. Biochemistry. 2018 Jul 31; 57(30):4583-4596. PMID: 30004693.
- Published on 6/25/2018
Klimtchuk ES, Prokaeva T, Frame NM, Abdullahi HA, Spencer B, Dasari S, Cui H, Berk JL, Kurtin PJ, Connors LH, Gursky O. Unusual duplication mutation in a surface loop of human transthyretin leads to an aggressive drug-resistant amyloid disease. Proc Natl Acad Sci U S A. 2018 07 10; 115(28):E6428-E6436. PMID: 29941560.
- Published on 4/3/2018
Jayaraman S, Gantz DL, Haupt C, Fändrich M, Gursky O. Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner. Chem Commun (Camb). 2018 Apr 03; 54(28):3532-3535. PMID: 29565436.
- Published on 12/25/2017
Madico G, Gursky O, Fairman J, Massari P. Structural and Immunological Characterization of Novel Recombinant MOMP-Based Chlamydial Antigens. Vaccines (Basel). 2017 Dec 25; 6(1). PMID: 29295593.
- Published on 7/29/2017
Prokaeva T, Akar H, Spencer B, Havasi A, Cui H, O'Hara CJ, Gursky O, Leszyk J, Steffen M, Browning S, Rosenberg A, Connors LH. Hereditary Renal Amyloidosis Associated With a Novel Apolipoprotein A-II Variant. Kidney Int Rep. 2017 Nov; 2(6):1223-1232. PMID: 29270531.
- Published on 7/25/2017
Jayaraman S, Gantz DL, Haupt C, Gursky O. Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis. Proc Natl Acad Sci U S A. 2017 08 08; 114(32):E6507-E6515. PMID: 28743750.
- Published on 6/20/2017
Frame NM, Jayaraman S, Gantz DL, Gursky O. Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a "molecular mop" in immune response. J Struct Biol. 2017 Dec; 200(3):293-302. PMID: 28645735.
- Published on 6/20/2017
Klimtchuk ES, Prokaeva TB, Spencer BH, Gursky O, Connors LH. In vitro co-expression of human amyloidogenic immunoglobulin light and heavy chain proteins: a relevant cell-based model of AL amyloidosis. Amyloid. 2017 Jun; 24(2):115-122. PMID: 28632419.
- Published on 12/31/2016
Das M, Wilson CJ, Mei X, Wales T, Engen JR, Gursky O. Structural stability and local dynamics in disease-causing mutants of human apolipoprotein a-I: what makes the protein amyloidogenic? Amyloid. 2017 Mar; 24(sup1):11-12. PMID: 28042708.
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