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D. Fernando                    Estrada

D. Fernando Estrada PhD

Department of Biochemistry

Assistant Professor

Specialty/Research Focus

Protein Function and Structure; Proteins and metalloenzymes; Vitamins and Trace Nutrient

 
Professional Summary:

Cytochrome P450 enzymes are ubiquitous catalysts that play integral roles in biochemical pathways throughout nature. In mammals, members of this class of enzyme serve a variety of functions that include drug metabolism, steroid biosynthesis and the activation and deactivation of vitamin D, to name a few. Cytochrome P450 enzymes are also heavily involved in bacterial and plant biochemistry.

The overall goal of my lab is to use a combination of biochemical and biophysical tools to investigate structure and function in cytochrome P450 enzymes, thereby contributing toward an understanding of how this important class of enzymes work as well as informing the design of novel drugs. This goal is divided between two efforts. First, we are interested in characterizing the ligand binding interactions of the enzyme CYP24A1, the principle enzyme responsible for deactivating vitamin D. Describing the interaction between CYP24A1 and vitamin D has the potential to illuminate how the vitamin D structure becomes modified at a particular site. This insight could impact the design of vitamin D analogs with benefits for an array of human health conditions, including bone density disorders, diabetes and chronic kidney disease (CKD). A parallel effort in my lab is a structural study of the enzyme CYP121 of Mycobacterium tuberculosis, the disease-causing pathogen in tuberculosis (TB). The resurgence of standard TB and the rise of drug-resistant forms of TB are quickly becoming a global pandemic, with TB claiming more lives worldwide in 2014 than HIV. CYP121 is essential for survival of the bacterium and thus has emerged as one of the more promising antitubercular drug targets.

Students and postdocs joining my lab will be exposed to a multidisciplinary set of research tools, including expression and purification of recombinant membrane protein, nuclear magnetic resonance, protein X-ray crystallography and P450 ligand binding assays.

Education and Training:
  • PhD, Biochemistry, University of Kansas (2011)
  • BS, Biochemistry, Kansas State University (1999)
  • AAS, Biology, Dodge City Community College (1996)
Employment:
  • Assistant Professor of Biochemistry, Biochemistry, University at Buffalo (2016-present)
  • NIH Postdoctoral Research Fellow, Medicinal Chemistry, University of Kansas (2011–2016)
  • Graduate Research Assistant, Molecular Biosciences, University of Kansas, College of Liberal Arts & Sciences (2006–2011)
  • U.S. Army Officer, United State Army (1999–2006)

Grants and Sponsored Research:
  • March 2015–July 2016
    Crystallographic and NMR studies of the human cytochrome P450 enzyme that inactivatesvitamin D
    National Institute of General Medical Sciences
    Role: Principal Investigator
    $193,334
  • November 2013–November 2015
    Ruth L. Kirschstein National Research Service Award; Application of solution NMR to membrane cytochrome P450 17A1
    National Institute of General Medical Sciences
    Role: Principal Investigator
    $122,264

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Contact Information

615 Biomedical Research Building
Department of Biochemistry
University at Buffalo
Buffalo, NY 14214
Phone: 716-829-2767
Fax: 716-829-2725
Email: dfestrad@buffalo.edu


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