Directed supramolecular surface assembly of SNAP-tag fusion proteins

D.A. Uhlenheuer, D. Wasserberg, C. Haase, H. Nguyen, J.H. Schenkel, J. Huskens, B.J. Ravoo, P. Jonkheijm, L. Brunsveld

Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikelAcademicpeer review

36 Citaten (Scopus)

Samenvatting

Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106¿M-1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements.
Originele taal-2Engels
Pagina's (van-tot)6788-6794
Aantal pagina's7
TijdschriftChemistry : A European Journal
Volume18
Nummer van het tijdschrift22
DOI's
StatusGepubliceerd - 2012

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