Chemistry at UNC Chapel Hill
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UNC-CH Collaborators
Dorothy Erie
Michael Falvo
Nobuyo Maeda
Mark Schoenfisch
Richard Superfine
 
  Susan T. Lord
  Professor and Adjunct Professor of Chemistry
 

stl@med.unc.edu
919-966-3548
919-966-6718 (fax)
821 Brinkhous-Bullitt

   
  Research Interests
  Role of Fibrinogen in Cardiovascular Diseases
   
  Professional Background
  Postdoctoral Fellow, Yale (1978-1980). Visiting Scientist, Uppsala University (1977-1978). Cornell University Medical College, Ph.D. Biochemistry (1977), Mount Holyoke College, B.A.-Chemistry (1967).
   
  Research Synopsis
  We study the blood clotting protein fibrinogen, its biochemistry and its role in disease. During clot formation soluble fibrinogen is converted to an insoluble fibrin matrix. Together fibrinogen and fibrin provide the framework in a blood clot, giving the clot shape, strength, flexibility and stability. (Curr Opin Hematol. 14:236, 2007). Our studies can be divided into four areas:
   
   
   
  We synthesize variant fibrinogens to correlate structure and function. We examine the changes in structure using X-ray crystallography. We examine the changes in function using many biochemical analyses; for example, we measure the kinetics of fibrin formation by absorbance at 350 nm. Our studies have provided insight into the nature of the interactions that mediate fibrin polymerization. (Biochemistry 46:5114, 2007).
   
   
  We examine the mechanical properties of fibrin fibers using a dual atomic force-fluorescence microscope. We form fluorescently-labeled fibers suspended on a corrugated surface. We use the atomic force microscope to pull on a fiber and record a video image of the stretched fiber. We found fibrin fibers are the strongest biological fibers. (Science 313:634. 2006).
   
   
  We explore the interactions of fibrinogen with biomaterials. When medical implants contact blood, fibrinogen is adsorbed onto the material surface, leading to pathological responses including formation of fibrin. We examine the interaction of fibrinogen with different surfaces using surface plasmon resonance. Our studies have shown that the conversion of surface fibrinogen to fibrin is lower on negatively charged relative to hydrophobic surfaces. (Acta Biomaterialia 3:663, 2007).
   
   
   
  We use patient samples and mouse models to examine the links between fibrinogen and disease. Epidemiological studies show elevated fibrinogen is a cardiovascular risk factor. Our studies with genetically modified mouse models showed that elevated fibrinogen does not alter the incidence of diet-induced atherosclerosis in mice. (Arterioscler Thromb Vasc Biol 23:130, 2003)
  Aortas from mice with elevated (B & C) or normal (D & E) fibrinogen.
Red stain shows fat deposits.
   
   
 
 
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Department of Chemistry
Campus Box 3290
Caudill and Kenan Laboratories
The University of North Carolina at Chapel Hill
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Phone: (919) 843-7100

 

Last Updated: September 7, 2007
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