Olga Gursky, PhD

Professor, Physiology & Biophysics

Olga Gursky
(617) 638-7894
700 Albany St Ctr for Adv Biomed Res

Biography

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.

Other Positions

  • Graduate Faculty (Primary Mentor of Grad Students), Boston University School of Medicine, Division of Graduate Medical Sciences

Education

  • Brandeis University, PhD
  • Moscow State University, MS

Publications

  • 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 Aug 08; 114(32):E6507-E6515. PMID: 28743750.

    Read at: PubMed
  • 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.

    Read at: PubMed
  • 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 Jun 20. PMID: 28645735.

    Read at: PubMed
  • 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.

    Read at: PubMed
  • Published on 12/31/2016

    Frame NM, Gursky O. Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks. Amyloid. 2017 Mar; 24(sup1):13-14. PMID: 28042712.

    Read at: PubMed
  • Published on 10/18/2016

    Jayaraman S, Sánchez-Quesada JL, Gursky O. Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases. Biochim Biophys Acta. 2017 Jan; 1863(1):200-210. PMID: 27768903.

    Read at: PubMed
  • Published on 10/15/2016

    Jayaraman S, Haupt C, Gursky O. Paradoxical effects of SAA on lipoprotein oxidation suggest a new antioxidant function for SAA. J Lipid Res. 2016 Dec; 57(12):2138-2149. PMID: 27744369.

    Read at: PubMed
  • Published on 5/24/2016

    Rull A, Jayaraman S, Gantz DL, Rivas-Urbina A, Pérez-Cuellar M, Ordóñez-Llanos J, Sánchez-Quesada JL, Gursky O. Thermal stability of human plasma electronegative low-density lipoprotein: A paradoxical behavior of low-density lipoprotein aggregation. Biochim Biophys Acta. 2016 09; 1861(9 Pt A):1015-24. PMID: 27233433.

    Read at: PubMed
  • Published on 3/6/2016

    Frame NM, Gursky O. Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks. FEBS Lett. 2016 Mar; 590(6):866-79. PMID: 26918388.

    Read at: PubMed
  • Published on 11/10/2015

    Das M, Wilson CJ, Mei X, Wales TE, Engen JR, Gursky O. Structural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic? J Mol Biol. 2016 Jan 29; 428(2 Pt B):449-62. PMID: 26562506.

    Read at: PubMed

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