Protective protein islands for the cytoskeleton
Prof. Stefan Diez celebrates 15th anniversary of his research group with BioNano Symposium
Zoltan Bognar, TRANSNETYX
Prof. Bernhard Wolfrum, Technical University of Munich, Munich School of Bioengineering & Forschungszentrum Jülich GmbH
On Bees and Humans - A Love Affair between Nature and Culture
Publication: Minimal Peptide Motif for Non-Covalent Peptide-Heparin Hydrogels
JACS - Journal of the American Chemical Society, 6 Feb 2013
Reduction of complexity of the extracellular matrix (ECM) to a non-covalent structure with minimal chemically defined components represents an attractive avenue for understanding the biology of the ECM. The resulting system could lead to the design of tailor-made biomaterials that incorporate varying functionalities. Negatively charged glycosaminoglycans are the major components of the ECM. Their interaction with positively charged proteins is important for dynamic three-dimensional scaffold formation and function. We designed and screened minimal peptide motifs whose conjugates with polyethylene glycol interact with heparin to form non-covalent hydrogels. Here we show the structure/function relationship of the (RA)n and (KA)n motifs and determined that both basic residues and the heparin-induced ?-helix formation are important for the assembly process. Simple rules allowed us to tune various aspects of the matrix system such as the gelation rates, biodegradability, rheological properties, and biofunctionality. The hydrogels can encapsulate cells and support cell survival.
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Robert Wieduwild, Mikhail V. Tsurkan, Karolina Chwalek, Priyanka Murawala, Mirko Nowak, Uwe Freudenberg, Christoph Neinhuis, Carsten Werner and Yixin Zhang: Minimal Peptide Motif for Non-covalent Peptide–Heparin Hydrogels, J. Am. Chem. Soc., 2013, 135 (8), pp 2919–2922
doi: 10.1021/ja312022uBack to News Ticker