Enzyme mediated site-specific surface modification

Langmuir. 2010 Jul 6;26(13):11127-34. doi: 10.1021/la1008895.


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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Factor XIIIa / chemistry
  • Hydrogels / chemistry
  • Mice
  • Microscopy
  • Models, Theoretical
  • Peptides / chemistry*
  • Polyethylene Glycols / chemistry
  • Polymers / chemistry*
  • Surface Properties
  • Transglutaminases / metabolism


  • Hydrogels
  • Peptides
  • Polymers
  • Polyethylene Glycols
  • Factor XIIIa
  • Transglutaminases