Quick Search:

uzh logo
Browse by:


Zurich Open Repository and Archive

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.

Accepted Version
View at publisher


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).


7 citations in Web of Science®
9 citations in Scopus®
Google Scholar™



174 downloads since deposited on 07 Jan 2011
13 downloads since 12 months

Detailed statistics

Additional indexing

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
Dewey Decimal Classification:170 Ethics
610 Medicine & health
Date:6 July 2010
Deposited On:07 Jan 2011 09:04
Last Modified:29 Nov 2013 15:37
Publisher:American Chemical Society
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

Users (please log in): suggest update or correction for this item

Repository Staff Only: item control page