Advanced Materials

Combinatorial Screening of Biomimetic Protein Affinity Materials

Authors

  • Trent R. Northen,

    1. Life Sciences Division Lawrence Berkeley National Laboratory 1 Cyclotron Road, Berkeley, CA 94720 (USA)
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  • Matthew P. Greving,

    1. Department of Chemistry and Biochemistry Biodesign Institute, Arizona State University Tempe, AZ 852 87 (USA)
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  • Neal W. Woodbury

    Corresponding author
    1. Department of Chemistry and Biochemistry Biodesign Institute, Arizona State University Tempe, AZ 852 87 (USA)
    • Department of Chemistry and Biochemistry Biodesign Institute, Arizona State University Tempe, AZ 85287 (USA).
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  • T.R.N. and M.P.G. contributed equally to this work, and were both supported by NSF IGERT Fellowships. This work was funded by The Biodesign Institute at Arizona State University, Department of Energy (grant DE-FC36-05GO15016 and DE-AC02-05CH11231), NSF (grant DGE-0114434), and NSF grant no. CHE-0131222 (mass spectrometer). We would also like to thank Paul Belcher for the SPR measurements, Rashaad Sidique, and the Center for Solid State Science at Arizona State University for SEM images. Supporting Information is available online from Wiley InterScience or from the authors.

Abstract

A patterned combinatorial library of peptide-grafted polymer affinity materials is screened for target protein binding. In situ light-directed synthesis is used to produce high-density libraries that allow for the screening in parallel within an area less than 1 cm2. From these libraries, specific peptide/polymer combinations are identified with very high target protein affinity, enabling facile detection of the target at concentrations in the low picomolar range in the presence of excess competitor.

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