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Angew Chem Int Ed Engl. 2014 Nov 10;53(46):12618-23. doi: 10.1002/anie.201404616. Epub 2014 Jul 28.

A chemoenzymatic approach to protein immobilization onto crystalline cellulose nanoscaffolds.

Author information

1
Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Strasse 4, 64287 Darmstadt (Germany).

Abstract

The immobilization of bioactive molecules onto nanocellulose leads to constructs that combine the properties of the grafted compounds with the biocompatibility and low cytotoxicity of cellulose carriers and the advantages given by their nanometer dimensions. However, the methods commonly used for protein grafting suffer from lack of selectivity, long reaction times, nonphysiological pH ranges and solvents, and the necessity to develop a tailor-made reaction strategy for each individual case. To overcome these restrictions, a generic two-step procedure was developed that takes advantage of the highly efficient oxime ligation combined with enzyme-mediated protein coupling onto the surface of peptide-modified crystalline nanocellulose. The described method is based on efficient and orthogonal transformations, requires no organic solvents, and takes place under physiological conditions. Being site-directed and regiospecific, it could be applied to a vast number of functional proteins.

KEYWORDS:

bioorthogonal protein immobilization; cellulose nanocrystals; enzyme catalysis; immobilization; ligation

PMID:
25070515
DOI:
10.1002/anie.201404616
[Indexed for MEDLINE]

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