Volume 92A, Issue 4 pp. 1329-1342

Profiles of carbohydrate ligands associated with adsorbed proteins on self-assembled monolayers of defined chemistries

Sucharita P. Shankar

Sucharita P. Shankar

Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, 313 Ferst Drive, Atlanta, Georgia 30332

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Inn Inn Chen

Inn Inn Chen

Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, 313 Ferst Drive, Atlanta, Georgia 30332

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Benjamin G. Keselowsky

Benjamin G. Keselowsky

George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, 313 Ferst Drive, Atlanta, Georgia 30332

Present address: J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, FL 32611.

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Andrés J. García

Andrés J. García

George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, 313 Ferst Drive, Atlanta, Georgia 30332

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Julia E. Babensee

Corresponding Author

Julia E. Babensee

Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, 313 Ferst Drive, Atlanta, Georgia 30332

Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, 313 Ferst Drive, Atlanta, Georgia 30332Search for more papers by this author
First published: 07 April 2009
Citations: 14

Abstract

Conserved protein–carbohydrate–lipid pathogen-associated molecular patterns (PAMPs) interact with cells of the innate immune system to mediate antigen recognition and internalization and activation of immune cells. We examined if analogous “biomaterial-associated molecular patterns” composed of proteins, specifically their carbohydrate modifications, existed on biomaterials, which can play a role in mediating the innate immune response to biomaterials. To probe for these carbohydrates in the adsorbed protein layer, as directed by the underlying biomaterial chemistry, self-assembled monolayers (SAMs) presenting CH3, OH, COOH, or NH2 were preincubated with serum/plasma, and the presence of carbohydrate ligands of C-type lectin receptors (CLRs) was investigated using lectin probes in an enzyme-linked lectin assay (ELLA). Presentation of CLR ligands was detected on control tissue culture polystyrene (TCPS). Absorbances of mannose or N-acetylglucosamine increased with decreasing incubating serum concentration, whereas absorbances of sialylated epitopes or fucose remained unchanged. Absorbances of α-galactose or N-acetylgalactosamine decreased with decreasing incubating serum concentration; β-galactose was undetectable. Among SAM endgroups, preincubation with 10% serum resulted in differential presentation of CLR ligands: higher α-galactose on COOH SAMs than NH2 or CH3 SAMs, highest complex mannose on NH2 SAMs, and higher complex mannose on OH SAMs than CH3 SAMs. Least sialylated groups were detected on CH3 SAMs. In summary, biomaterial chemistry may regulate protein adsorption and hence unique presentation of associated carbohydrates. The ultimate goal is to identify the effects of protein glycosylations associated with biomaterials in stimulating innate immune responses. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res, 2010

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