Oriented immobilization of proteins on solid supports for use in biosensors and biochips: a review View Full Text


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Article Info

DATE

2016-01

AUTHORS

Yingshuai Liu, Jie Yu

ABSTRACT

Immobilization of proteins on a solid support is critical with respect to the fabrication and performance of biosensors and biochips. Protein attachment with a preferable orientation can effectively avoid its denaturation and keeps its active sites fully exposed to solution, thus maximally preserving the bioaffinity or bioactivity. This review (with 140 refs.) summarises the recent advances in oriented immobilization of proteins with a particular focus on antibodies and enzymes. Following an introduction that describes reasons for oriented immobilization on (nano)surfaces, we summarize (a) methods for (bio)chemical affinity-mediated oriented immobilization (with sections on immunoglobulin G (IgG)-binding protein as the capture ligand, DNA-directed immobilization, aptamer- and peptide-mediated immobilization, affinity ligand and fusion tag-mediated immobilization, material-binding peptide-assisted immobilization); (b) methods for covalent oriented immobilization (with sections on immobilization via cysteine residues or cysteine tags, via carbohydrate moieties; via enzyme fusion or enzymatic catalysis, and via nucleotide binding sites of antibodies); (c) methods based on molecular imprinting techniques; (d) methods for characterization of oriented immobilized proteins; and then make conclusions and give perspectives. Graphical AbstractThis review summarises recent advances in oriented immobilization of proteins based on strategies via bio−/chemical affinity, covalent bonding, and molecular imprinting techniques. Advantages and disadvantages of each approach are discussed. This review summarises recent advances in oriented immobilization of proteins based on strategies via bio−/chemical affinity, covalent bonding, and molecular imprinting techniques. Advantages and disadvantages of each approach are discussed. More... »

PAGES

1-19

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    http://scigraph.springernature.com/pub.10.1007/s00604-015-1623-4

    DOI

    http://dx.doi.org/10.1007/s00604-015-1623-4

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