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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-40388

Sala, A; Ehrbar, M; Trentin, D; Schoenmakers, R G; Vörös, J; Weber, F E (2010). Enzyme mediated site-specific surface modification. Langmuir, 26(13):11127-11134.

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Abstract

Stable tethering of bioactive peptides like RGD to surfaces can be achieved via chemical bonding, biotin streptavidin interaction, or photocross-linking. More challenging is the immobilization of proteins, since methods applied to immobilize peptides are either not specific or versatile enough or might even compromise the protein's bioactivity. To overcome this limitation, we have employed a scheme that by enzymatic (transglutaminase) reaction allows the site-directed and site-specific coupling of growth factors and other molecules to nonfouling poly(L-lysine)-graft-poly(ethylene glycol) (PLL-g-PEG) coated surfaces under physiological conditions. By our modular and flexible design principle, we are able to functionalize these surfaces directly with peptides and growth factors or precisely position poly(ethylene glycol) (PEG)-like hydrogels for the presentation of growth factors as exemplified with vascular endothelial growth factor (VEGF).

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Division of Surgical Research
04 Faculty of Medicine > University Hospital Zurich > Clinic for Obstetrics
04 Faculty of Medicine > Center for Dental Medicine > Clinic for Cranio-Maxillofacial Surgery
04 Faculty of Medicine > Institute of Biomedical Engineering
DDC:170 Ethics
610 Medicine & health
Language:English
Date:6 July 2010
Deposited On:07 Jan 2011 09:04
Last Modified:29 Nov 2013 15:37
Publisher:American Chemical Society
ISSN:0743-7463
Additional Information:This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, copyright © American Chemical Society after peer review and technical editing by the publisher.
Publisher DOI:10.1021/la1008895
PubMed ID:20545368
Citations:Web of Science®. Times Cited: 4
Google Scholar™
Scopus®. Citation Count: 5

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