Research & Publications
Dr. Bunick uses structural biology techniques called x-ray crystallography, nuclear magnetic resonance, and cryo-electron microscopy to determine the high resolution, three-dimensional structures of proteins important to both normal and diseased skin. Knowing the structure of various skin proteins enables a better understand of how a protein functions in normal and diseased skin states. Ultimately, it may lead to the development of novel therapies.
Specialized Terms: structural biology of skin proteins; x-ray crystallography; epidermal structure and function; structure-based drug design; cryo-EM; NMR
Extensive Research Description
Dr. Christopher Bunick, MD, PhD, is an Associate Professor of Dermatology performing dermatologic research studying the three-dimensional structures of skin-related proteins using primarily x-ray crystallography and cryo-electron microscopy. Dr. Bunick has 25 years of experience in the field of structural biology. He leads a structural biology research program in the dermatology field, with a specific niche: “atomic resolution dermatology.” Dr. Bunick’s research focuses on determining the atomic resolution structures of proteins and protein complexes essential to formation of a functional human skin barrier. He uses x-ray crystallography and cryo-electron microscopy to determine the high resolution, three-dimensional structures of proteins important to both normal and diseased skin. Knowing the structure of various skin proteins enables a better understanding of how a protein functions in normal and diseased skin states. Ultimately, it may lead to the development of novel therapies.
Two recent proteins studied are human profilaggrin and the keratin 1/10 complex because of their importance to skin barrier integrity and association with clinically relevant skin diseases. The NIH/NIAMS website estimates up to 90 million Americans suffer from some form of atopic dermatitis. Atopic dermatitis and other forms of severely dry skin, such as ichthyosis vulgaris, are associated with defects or mutations in profilaggrin and its processed fragment, filaggrin. Similarly, mutations mapped to keratins 1 or 10 are linked to several clinical disorders of keratinization (keratinopathies). Work on these proteins led to a 2.2 Å resolution crystal structure of the profilaggrin S100 calcium-binding domain and several 2.0 Å to 3.3 Å resolution crystal structures of complexes between the 1B and 2B helices of K1 and K10. Dr. Bunick currently is funded by the NIH/NIAMS (K08 and R03 Awards) and research grants from the Patterson Trust and Almirall. His laboratory is open to students and post-docs motivated by and passionate for applying biochemistry and structural biology to skin disease.
Biochemistry; Biophysics; Dermatitis, Atopic; Dermatology; Epidermis; Intermediate Filaments; Keratins; Molecular Biology; Skin; Ichthyosis Vulgaris; Crystallography, X-Ray; Computational Biology; Proteomics
Public Health Interests