{"id":21600,"date":"2023-09-13T11:10:22","date_gmt":"2023-09-13T15:10:22","guid":{"rendered":"http:\/\/www.bumc.bu.edu\/ppb\/?page_id=21600"},"modified":"2025-10-08T13:55:46","modified_gmt":"2025-10-08T17:55:46","slug":"the-gursky-lab","status":"publish","type":"page","link":"https:\/\/www.bumc.bu.edu\/ppb\/the-gursky-lab\/","title":{"rendered":"The Gursky Lab"},"content":{"rendered":"<p><img src=\"\/ppb\/files\/2025\/08\/Gursky-Lab-Banner-1-1.jpg\" alt=\"Gursky Lab banner\" width=\"1200\" height=\"162\" loading=\"eager\" decoding=\"async\" style=\"width: 100%; height: auto;\" \/><br \/>\n<button onclick=\"scrollToTop()\" id=\"backToTopBtn\" title=\"Go to top\" style=\"display: none; position: fixed; bottom: 80px; right: 20px; z-index: 1000; font-size: 16px; border: none; outline: none; background-color: #333; color: white; cursor: pointer; padding: 5px 16px; border-radius: 8px; box-shadow: 0 4px 12px rgba(0, 0, 0, 0.3);\"><br \/>\n<strong>Top\u2191<br \/>\n<\/strong><\/button><\/p>\n<nav class=\"site-nav\" style=\"position: sticky; top: 0; width: 100%; background: #fff; border-bottom: 1px solid #eee; z-index: 50; box-shadow: 0 2px 4px rgba(0,0,0,0.05);\">\n<div style=\"max-width: 1200px; margin: 0 auto; padding: 1rem 2rem;\">\n<ul style=\"display: flex; justify-content: center; gap: 2rem; list-style: none; margin: 0; padding: 0; font-weight: 600; font-size: 1.3rem;\">\n<li><a href=\"#research\" style=\"color: #333; text-decoration: none;\">Research<\/a><\/li>\n<li><a href=\"#group\" style=\"color: #333; text-decoration: none;\">Group<\/a><\/li>\n<li><a href=\"#publications\" style=\"color: #333; text-decoration: none;\">Publications<\/a><\/li>\n<li><a href=\"#teach\" style=\"color: #333; text-decoration: none;\">Teaching<\/a><\/li>\n<li><a href=\"#contact\" style=\"color: #333; text-decoration: none;\">Contact<\/a><\/li>\n<\/ul>\n<\/div>\n<\/nav>\n<div style=\"max-width: 1200px; margin: 0 auto 2rem auto; text-align: center;\">\n<div style=\"max-width: 1200px; margin: 2rem auto; padding: 1.5rem 2rem; border-radius: 0.5rem;\">\n<p style=\"font-size: 1.1rem; line-height: 1.8; color: #333; text-align: justify; margin: 0;\"><strong>Welcome to the Gursky Lab at Boston University School of Medicine!<\/strong> Our research focuses on the structural and biophysical mechanisms of lipoprotein metabolism and protein misfolding. Using techniques such as cryo-electron microscopy, spectroscopy, and computational modeling, we aim to uncover how these molecular processes contribute to cardiovascular disease and amyloidosis. Through interdisciplinary and collaborative research, we strive to advance both fundamental understanding and translational applications.<\/p>\n<p>&nbsp;<\/p>\n<p style=\"text-align: left;\">Last Updated: Aug 2025<\/p>\n<div style=\"text-align: center; margin-top: 1.5rem;\"><img src=\"\/ppb\/files\/2025\/08\/Gursky-Lab-Photo-Pt.2.jpg\" alt=\"Gursky Lab Group Photo\" style=\"width: 100%; border-radius: 0.5rem; box-shadow: 0 2px 8px rgba(0,0,0,0.1);\" \/><span style=\"color: #777777; font-size: 0.9rem; font-style: italic;\">Crowns are our lab photo tradition!<\/span><\/div>\n<\/div>\n<section id=\"research\" style=\"padding: 3rem 1rem; background: #f9f9f9;\">\n<h2 style=\"text-align: center; font-size: 2.5rem; margin-bottom: 2rem;\">Research<\/h2>\n<h5>Free energy barriers in lipoprotein stability and remodeling<\/h5>\n<p style=\"text-align: justify;\">Plasma lipoproteins are nanoparticles containing several proteins and several hundred lipids, which mediate lipid transport and metabolism and are essential in cardiovascular health and disease. We uncovered that all major lipoprotein classes including high-, low- and very-low-density lipoproteins (a.k.a. Good and Bad Cholesterol) are stabilized by high free energy barriers. We developed biophysical approach to measure these barriers. By using circular dichroism spectroscopy, turbidity, electron microscopy, gel filtration and biochemical methods, we demonstrated that these barriers involve lipoprotein fusion and protein dissociation similar to those involved in metabolic lipoprotein remodeling. Studies of lipoprotein stability pioneered by our lab helped obtain relative rates of remodeling of lipoprotein classes and subclasses and assess how various in vivo factors can modulate these rates. One example is current kinetic studies of aggregation and fusion of low-density lipoproteins, which are thought to trigger atherosclerosis.<\/p>\n<figure style=\"max-width: 800px; margin: 2rem auto; text-align: center;\"><img src=\"\/ppb\/files\/2023\/05\/Picture6.jpg\" alt=\"LDL fusion image\" style=\"width: 100%; border-radius: 0.5rem; box-shadow: 0 2px 8px rgba(0,0,0,0.1);\" \/><figcaption style=\"font-size: 0.9rem; margin-top: 1rem; color: #444;\"><strong>Structural stability and fusion of low-density lipoproteins<\/strong><br \/>\n<em>Research by Mengxiao Lu, PhD in Biophysics 2014<\/em> Lu M, Gantz DL, Herscovitz H, Gursky O.<br \/>\n<span style=\"color: #cc0000;\">J Lipid Res. 2012; 53(10):2175-2185<\/span> <span style=\"color: #cc0000;\">Biomol Concepts. 2013; 4(5):501-518<\/span><\/figcaption><\/figure>\n<p>&nbsp;<\/p>\n<h4><a id=\"earlywork\" name=\"earlywork\"><\/a><br style=\"clear: both;\" \/>Protein misfolding and amyloid<\/h4>\n<p style=\"text-align: justify;\">Our studies have revealed novel aspects of misfolding and aggregation of amyloid-forming proteins. We were the first to report heat-induced beta-sheet folding and aggregation in amyloid-beta peptide and to demonstrate kinetic control in the misfolding and aggregation of immunoglobulin light chain. We proposed the molecular mechanisms for misfolding and aggregation of naturally occurring mutants of apolipoproteins A-I and A-II that cause amyloid disease in humans. Our approach combines circular dichroism and fluorescence spectroscopy, turbidity, calorimetry, electron microscopy with biochemical and immunochemical methods and structural and bioinformatic approaches. Local, national and international collaborations provide invaluable expertise in other methods of structural and cell biology and in translational research.<\/p>\n<figure style=\"max-width: 800px; margin: 2rem auto; text-align: center;\"><img src=\"\/ppb\/files\/2023\/05\/FEBS-J-cover-figure-page-001-779x1024.jpg\" alt=\"FEBS Journal cover figure: ApoA-I amyloidogenic mutations study\" width=\"592\" height=\"778\" loading=\"lazy\" decoding=\"async\" style=\"width: 100%; border-radius: 0.5rem; box-shadow: 0 2px 8px rgba(0,0,0,0.1);\" \/><figcaption style=\"font-size: 0.9rem; margin-top: 1rem; color: #444;\"><strong>Research by Madhurima Das, PhD Candidate in Biophysics<\/strong><br \/>\nAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing \u2014 a common mechanism of apoA-I misfolding in familial amyloidosis and atherosclerosis. Das M, Mei X, Jayaraman S, Atkinson D, Gursky O.<br \/>\n<span style=\"color: #cc0000;\"><em>FEBS J.<\/em> 2014; 281(11):2525\u20132542<\/span><\/figcaption><\/figure>\n<p>Recently, we investigated the structural mechanisms underlying amyloid light-chain (AL) amyloidosis, a protein misfolding disorder driven by aggregation of monoclonal immunoglobulin light chains (LCs). Using high-resolution cryogenic electron microscopy (cryo-EM), we resolved the fibril architecture of cardiac AL-224L amyloid belonging to the overrepresented \u03bb6 LC family. <!-- Amyloid Figures Segment --><\/p>\n<section style=\"padding: 3rem 1rem; background: #ffffff; max-width: 1000px; margin: 0 auto;\"><!-- Right-aligned Cryo-EM figure with caption --><\/p>\n<div style=\"float: right; width: 50%; margin-left: 2rem; margin-bottom: 2rem;\">\n<p><img src=\"\/ppb\/files\/2025\/08\/Amyloid-Figures-.jpg\" alt=\"Cryo-EM structure of AL252L fibrils\" style=\"width: 100%; border-radius: 0.5rem; box-shadow: none;\" \/><\/p>\n<p style=\"font-size: 0.95rem; color: #555; margin-top: 0.5rem; line-height: 1.5;\"><strong>Cryo-EM structure of AL252L fibrils derived from liver tissue by <b>Noorul Huda, PhD<\/b>.<\/strong> (A) Side view of the AL252L fibril cryo-EM density map at 3.5 \u00c5 resolution showing characteristic 4.79 \u00c5 helical rise of \u03b2-strands along the fibril axis. (B) Cross-sectional view of the density map (blue) with the expected backbone trace (orange), highlighting disordered region with dotted line.<\/p>\n<\/div>\n<p><!-- Centered GIF (left-side column) --><\/p>\n<div style=\"width: 45%; float: left; margin-bottom: 2rem;\"><img src=\"\/ppb\/files\/2025\/08\/Amyloid-Model-Gursky-Lab.gif\" alt=\"Amyloid Model\" style=\"width: 70%; border-radius: 0.5rem; box-shadow: none;\" class=\"alignnone\" \/><\/div>\n<div style=\"clear: both;\"><\/div>\n<p><!-- Centered SAA Exposures Image with Caption --><\/p>\n<div style=\"text-align: center; margin-top: 2rem;\">\n<p><img src=\"\/ppb\/files\/2025\/08\/Screenshot-2025-08-23-at-12.11.44\u202fPM.jpg\" alt=\"Serum Amyloid A exposures\" style=\"max-width: 100%; border-radius: 0.5rem; box-shadow: none;\" \/><\/p>\n<p style=\"font-size: 0.95rem; color: #555; margin-top: 0.5rem;\"><strong>Micrographs\/Exposures representing fibrils of Serum Amyloid A with CSA<\/strong><\/p>\n<\/div>\n<\/section>\n<p style=\"text-align: left;\">Dr. Gursky has authored more than 50 peer-reviewed journal articles and several book chapters (click <a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/?term=(gursky+o%5BAuthor%5D\">here<\/a> for Pubmed list). She is an elected Fellow of the American Heart Association (AHA), an editorial board member of the Journal of Lipid Research, and a frequent reviewer for NIH, NSF, AHA and other national, international and private agencies. She serves as a member of the Biophysics of Biological Membranes (BBM) study section at NIH. She is an editor of a book \u201cLipids in Protein Misfolding\u201d in preparation for publication by Springer in 2015. She has served as a visiting professor at the Indian Institute of Technology (IIT) Bombay. She is teaching major PhD-level courses and is involved in graduate admissions and mentoring.<\/p>\n<p style=\"text-align: justify;\">Dr. Gursky has mentored a number of pre- and postdoctoral trainees who went on to their own successful careers in life sciences. All past PhD students graduated in 5 to 5 \u00bd years with a couple of first-author publications. We have a track record of maintaining a family-friendly environment and attracting women in science.<\/p>\n<section id=\"group\" style=\"padding: 4rem 2rem; background: #fff; max-width: 900px; margin: auto;\">\n<h2 style=\"text-align: center; font-size: 2.5rem; margin-bottom: 2rem;\">The Group<\/h2>\n<ul style=\"list-style: none; padding: 0; font-size: 1.05rem; line-height: 1.8; color: #333;\">\n<li style=\"text-align: center;\"><strong>Olga Gursky, PhD<\/strong> \u2013 Principal Investigator, Professor<\/li>\n<li><\/li>\n<li style=\"text-align: center;\"><strong>Shobini Jayaraman, PhD<\/strong> \u2013 Senior Scientist<\/li>\n<li><\/li>\n<li style=\"text-align: center;\"><strong>Noorul Huda, PhD<\/strong> \u2013 Postdoctoral Researcher<\/li>\n<li><\/li>\n<li style=\"text-align: center;\"><strong>Kyeongseo Choi<\/strong> \u2013 Undergraduate RA\/Webmaster<\/li>\n<\/ul>\n<\/section>\n<h4><\/h4>\n<h4><\/h4>\n<h4 style=\"text-align: center;\">Collaborations<\/h4>\n<p style=\"text-align: left;\"><strong>Dr. Haya Herscovitz<\/strong> \u2013 BUSM Physiology &amp; Biophysics. Apolipoprotein cell biology.<\/p>\n<p style=\"text-align: left;\"><strong>Dr. David Atkinson<\/strong> \u2013 BUSM Physiology &amp; Biophysics. ApoA-I mutants.<\/p>\n<p style=\"text-align: left;\"><strong>Dr. Catherine E. Costello<\/strong> \u2013 BUSM Mass Spectrometry Resource. Ion mobility MS.<\/p>\n<p style=\"text-align: left;\"><strong>Dr. John R. Engen<\/strong> \u2013 Northeastern University. H-D exchange mass spectrometry.<\/p>\n<p style=\"text-align: left;\"><strong>Dr. Marcus F\u00e4ndrich<\/strong> \u2013 University of Ulm, Germany. Serum Amyloid A.<\/p>\n<p style=\"text-align: left;\"><strong>Dr. Jos\u00e9 Luis S\u00e1nchez-Quesada<\/strong> &#8211; Int. de Recerca, Barcelona Spain. Electronegative LDL <a id=\"trainees\" name=\"trainees\"><\/a><\/p>\n<h5 style=\"text-align: center;\"><a id=\"MMLS\" name=\"MMLS\"><\/a>Lab Alumni<\/h5>\n<p style=\"text-align: left;\"><strong>Emily Lewkowicz, PhD <\/strong><\/p>\n<p style=\"text-align: left;\"><b>Madhurima Das, PhD<\/b><\/p>\n<p style=\"text-align: left;\"><b>Isabel Morgado, PhD<\/b><\/p>\n<p style=\"text-align: left;\"><b>Donald Gantz<\/b><\/p>\n<h4 style=\"text-align: left;\"><\/h4>\n<section id=\"publications\" style=\"padding: 4rem 2rem; background: #ffffff; max-width: 900px; margin: auto;\">\n<h2 style=\"text-align: center; font-size: 2.5rem; margin-bottom: 2rem;\">Publications<\/h2>\n<ul style=\"list-style: none; padding: 0; font-size: 1.05rem; line-height: 1.8; color: #333;\">\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>An unusual phenotype of hereditary AApoAI amyloidosis caused by a novel Asp20Tyr substitution is linked to pH-dependent aggregation of apolipoprotein AI<\/strong><br \/>\nT Prokaeva, S Jayaraman, E Klimtchuk, N Burke, B Spencer, D Nedelkov, <strong style=\"color: #005599;\">O Gursky<\/strong><br \/>\n<em>Biochimica et Biophysica Acta (BBA) &#8211; Molecular Basis of Disease<\/em>, 2025<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Serum Amyloid A Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis<\/strong><br \/>\nS Jayaraman, A Urdaneta, M Fandrich, <strong style=\"color: #005599;\">O Gursky<\/strong><br \/>\n<em>Journal of Molecular Biology<\/em>, 2025<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Cryo-EM of cardiac AL-224L amyloid reveals shared features in \u03bb6 light chain fibril folds<\/strong><br \/>\nCW Hicks, T Prokaeva, B Spencer, S Jayaraman, N Huda, S Wong, <strong style=\"color: #005599;\">O Gursky<\/strong><br \/>\n<em>bioRxiv<\/em>, 2025<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Elucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A<\/strong><br \/>\nCB Abraham, E Lewkowicz, <strong style=\"color: #005599;\">O Gursky<\/strong>, JE Straub<br \/>\n<em>Biochemistry<\/em>, 2024<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Conformational differences in the light chain constant domain of immunoglobulin G and free light chain may influence proteolysis in AL amyloidosis<\/strong><br \/>\nES Klimtchuk, T Prokaeva, BH Spencer, S Wong, S Ghosh, A Urdaneta, <strong style=\"color: #005599;\">O Gursky<\/strong><br \/>\n<em>Journal of Molecular Biology<\/em>, 2024<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Science around the world<\/strong><br \/>\nA Plaza-Florido, <strong style=\"color: #005599;\">O Gursky<\/strong>, ML Herrera, CD Moschopoulos, Y Sohrabi<br \/>\n<em>Trends in Molecular Medicine<\/em>, 2024<\/li>\n<li style=\"margin-bottom: 1.5rem; text-align: justify;\"><strong>Amyloid and collagen templates in aortic valve calcification<\/strong><br \/>\nS Jayaraman, N Narula, J Narula, <strong style=\"color: #005599;\">O Gursky<\/strong><br \/>\n<em>Trends in Molecular Medicine<\/em>, 2024<\/li>\n<\/ul>\n<\/section>\n<h2 id=\"teach\" style=\"text-align: center; font-size: 2.2rem; margin: 3rem 0 2rem 0;\">Teaching<\/h2>\n<p style=\"text-align: left;\"><b>GMS FC711 Foundations in Biomedical Sciences I: Protein Structure, Catalysis and Interaction<\/b> The second module of the Foundations in Biomedical Science course provides students with a quantitative understanding of protein structure, function, posttranslational modifications and the turnover of proteins in the cell. In addition, students gain facility with thermodynamics, catalysis, kinetics and binding equilibria. <b><\/b><\/p>\n<p style=\"text-align: left;\"><b>FC708 Professional Development Skills<\/b><a href=\"http:\/\/www.bu.edu\/academics\/gms\/courses\/gms-fc-708\/\"><b> <\/b><\/a> The objective of this course is to extend students&#8217; education beyond the traditional biomedical course content so as to enable students to develop critical professional skills. Consideration is given to presentation skills, issues of compliance\/ethics &amp; the law as well as personal professional development. The course draws on a wide variety of experts throughout the university.<\/p>\n<p style=\"text-align: left;\"><b>GMS BY 763<\/b><b> Foundations of Biophysics and Structural Biology II<\/b> This graduate level course provides a thorough grounding in the theory and major experimental methods of Biophysics and Structural Biology. The course covers thermodynamic and spectroscopic methods, computational biology and structural NMR.<\/p>\n<p style=\"text-align: left;\"><b>GMS BY 871, 872<\/b><b> Biophysics Seminar<\/b> This is a special topics seminar series for first and second year graduate students. Each student presents several papers per semester describing the background, the specific methods, the results, the conclusions of the authors, and a critique of the work.<\/p>\n<h5>Links:<\/h5>\n<p><a href=\"https:\/\/profiles.bu.edu\/Olga.Gursky\">BU Profile<\/a><\/p>\n<p><a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=gursky+o&amp;sort=date\">PubMed<\/a><\/p>\n<p><a href=\"https:\/\/www.researchgate.net\/profile\/Olga-Gursky\">ResearchGate<\/a><\/p>\n<section id=\"contact\" style=\"padding: 4rem 2rem; background: #fff; max-width: 900px; margin: auto;\">\n<h2 style=\"text-align: center; font-size: 2.2rem; margin-bottom: 2rem;\">Contact Us<\/h2>\n<address style=\"font-size: 1.05rem; line-height: 1.8; color: #333; text-align: center;\">Department of Pharmacology, Physiology &amp; Biophysics Chobanian &amp; Avedisian School of Medicine 700 Albany Street, W302D, Boston MA 02118-2526<\/address>\n<address style=\"font-size: 1.05rem; line-height: 1.8; color: #333; text-align: center;\"><strong>Phone:<\/strong> (617)358-8468 (Office) | (617)358-8467 (Lab)<\/address>\n<address style=\"font-size: 1.05rem; line-height: 1.8; color: #333; text-align: center;\"><strong>Email:<\/strong> <a href=\"mailto:gursky@bu.edu\">gursky\\at\\bu.edu<\/a><\/address>\n<\/section>\n<footer style=\"text-align: center; font-size: 0.9rem; color: #888; padding: 2rem;\">\u00a9 2025 Gursky Lab | Boston University<\/footer>\n<\/section>\n<p><script>\r\n\/\/ Show\/hide the button based on scroll position\r\nwindow.onscroll = function() {\r\n  const btn = document.getElementById(\"backToTopBtn\");\r\n  if (document.body.scrollTop > 300 || document.documentElement.scrollTop > 300) {\r\n    btn.style.display = \"block\";\r\n  } else {\r\n    btn.style.display = \"none\";\r\n  }\r\n};\r\n\r\n\/\/ Smooth scroll to top\r\nfunction scrollToTop() {\r\n  window.scrollTo({\r\n    top: 0,\r\n    behavior: 'smooth'\r\n  });\r\n}\r\n<\/script><\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>Top\u2191 Research Group Publications Teaching Contact Welcome to the Gursky Lab at Boston University School of Medicine! Our research focuses on the structural and biophysical mechanisms of lipoprotein metabolism and protein misfolding. Using techniques such as cryo-electron microscopy, spectroscopy, and computational modeling, we aim to uncover how these molecular processes contribute to cardiovascular disease and [&hellip;]<\/p>\n","protected":false},"author":1811,"featured_media":0,"parent":0,"menu_order":42,"comment_status":"closed","ping_status":"closed","template":"page-templates\/no-sidebars.php","meta":[],"_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21600"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/users\/1811"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/comments?post=21600"}],"version-history":[{"count":49,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21600\/revisions"}],"predecessor-version":[{"id":21607,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21600\/revisions\/21607"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/media?parent=21600"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}