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  • Curtis F. Brewer, Ph.D.

Curtis F. Brewer, Ph.D.

Curtis F. Brewer

Professor, Department of Molecular Pharmacology

Professor, Department of Microbiology & Immunology

Area of Research: Biochemical and biophysical analysis of lectin binding

Contact Information

718.430.2227fred.brewer@einsteinmed.org

Albert Einstein College of Medicine
Jack and Pearl Resnick Campus

1300 Morris Park Avenue
Forchheimer Building, Room 206
Bronx, NY 10461

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More Resources: Department of Molecular Pharmacology

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Professional Interests

Cell surface carbohydrates have been demonstrated to be involved in a variety of biological recognition phenomena including cellular recognition and adhesion, regulation of inflammation, control of cell growth and metastasis. Although the structures of many of these carbohydrates have been elucidated, relatively little is known about their molecular recognition properties other than their interactions with glycosylases and lectins. Lectins are carbohydrate-binding proteins that are widely found in nature including plants, animals and pathogenic organisms. Lectins and the cell surface glycans of glycoproteins and glycolipids play important roles in cellular homeostasis and innate and adaptive immunity. Our research includes characterizing the biophysical and biochemical properties of lectins and their interactions with multivalent cellular glycans. We are also investigating the self-binding properties of carbohydrate tumor antigens and have presented evidence for their involvement in oncogenesis. Techniques used to explore these interactions include isothermal titration microcalorimetry, x-ray crystallography, atomic force microscopy and optical tweezers.


Selected Publications

Sletmoen, M., Gerken, T. A., Stokke, B. T., Burchell, J. and Brewer, C. F., Tn and STn are members of a family of carbohydrate tumor antigens that possess carbohydrate-carbohydrate interactions. Glycobiology 28; 437 (2018).

Dam, T. K., Fan, N., Talaga, M. L., Brewer, C. F., Stoichiometry regulates macromolecular recognition and supramolecular assembly: examples from lectin-glycoconjugate interaction, (Atwood, J. L., ed.) In., Comprehensive Supramolecular Chemistry II, Oxford: Elsevier, vol. 8, pp. 161–177 (2017).

Haugstad, K. E., Hadjialirezaei, S., Stokke, B. T., Brewer, C. F., Gerken, T. A., Burchell, J., Picco, G.  and Sletmoen, M., Interactions of mucins including MUC1 that possess the Tn or sialyl Tn cancer antigens are due to GalNAc – GalNAc interactions. Glycobiology 26; 1338 (2016).

Dam, T. K., Talaga, M. L., Fan, N. and Brewer C. F., Measuring multivalent binding interactions by isothermal titration calorimetry. (Feig, A. L., ed.) Calorimetry, Methods Enzymol., Vol. 567, Academic Press, New York, pp. 71-98 (2016).

Haugstad, K. E., Stokke, B. T., Gerken, T. A., Brewer, C. F. and Sletmoen, M., Single molecule study of heterotypic interactions between mucins possessing the Tn cancer antigen. Glycobiology 25; 524 (2015).

Brewer, C. F., Glycosylation Density in Cellular Homeostasis, Glycoscience: Biology and Medicine, (Taniguchi, N., Endo, E., Hart, G.W., Seeberger, P. and Wong, C.-H., eds.), Springer, Japan, pp. 661- 666 (2015).

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