U.S. Department of Health and Human Services
 

 Contact Info

 
Tel: 301-496-9893
Email: jmsayer@niddk.nih.gov
 

 Select Experience

 
  • Research ChemistLCP, NIDDK, NIH2007-present
  • Research ChemistLBC, NIDDK, NIH1985-2007
  • Special ExpertLBC, NIDDK, NIH1979-1985
  • Guest WorkerLBC, NIDDK, NIH1979-1983
  • Senior Research AssociateBrandeis University1969- 1974
  • NIH Postdoctoral FellowBrandeis University1967-1969
  • Ph.D.Yale University1967
 

 Related Links

 

    Jane M. Sayer, Ph.D.

    Research Chemist, Office of the Chief, Laboratory of Chemical Physics
    Specialties
    • Chemistry/Chemical Biology
    • Molecular Biology/Biochemistry
    Research Summary/In Plain Language

    Research Summary

    Research Goal

    The goal of my research is to gain a more complete understanding of the complex processes involved in spatiotemporal regulation of retroviral maturation and propagation.  This will help researchers identify novel strategies to target drug-resistant viral strains.​

    Current Research

    I am a member of the Protein Engineering and Chemistry Group within the Laboratory of Chemical Physics.  We apply kinetics, thermodynamics, and other biochemical and physicochemical approaches to elucidate enzymatic reaction mechanisms and protein-protein and protein-small molecule interactions.  We carry out ongoing studies on retroviral proteases (PR).  Specific interests include the mechanism and inhibition of retroviral PR maturation from its Gag-Pol polyprotein precursor.  Our findings may help to identify inhibitors that target the folding or transient dimerization of the PR precursor and to provide novel approaches to overcoming drug resistance.

    Prior to 2007, my research in the Section on Oxidation Mechanisms of the Laboratory of Bioorganic Chemistry focused on the organic chemistry and biochemistry of diol epoxides resulting from mammalian oxidative metabolism of carcinogenic polycyclic aromatic hydrocarbons (PAHs).  PAHs are widespread environmental pollutants.  Diol epoxides react with purine bases in DNA to form covalent adducts.  This results in erroneous DNA replication, a potential mechanism for initiation of cancer.  Our primary interests were in the reactivity and reaction mechanisms of the PAH diol epoxides.  We also studied the synthesis, purification, and spectroscopic characterization of modified oligonucleotides containing specific PAH adducts.  These studies were carried out in collaboration with biochemists, nuclear magnetic resonance spectroscopists, and crystallographers.  Our research examined the effects of these adducts on the replication of DNA by polymerases and on DNA processing by other enzymes, such as helicases and topoisomerases.

    Applying our Research

    The long-term survival of HIV-positive patients, which has been made possible because of successful ongoing drug therapy, may be jeopardized by the selection of resistant mutants under drug pressure.  Gaining a detailed understanding of the mechanisms of retroviral maturation will provide insights that researchers can use to develop new approaches to circumvent drug resistance and prolong lives.

    Need for Further Study

    Early events in retroviral maturation need to be better understood on a molecular level through the use of advanced biochemical and biophysical techniques.