Powerful Protein Binders from Designed Polypeptides and Small Organic Molecules—A General Concept for Protein Recognition (pages 1823–1827)
Dr. Lotta T. Tegler, Dr. Guillaume Nonglaton, Dr. Frank Büttner, Prof. Karin Caldwell, Tony Christopeit, Prof. U. Helena Danielson, Dr. Karin Fromell, Dr. Thomas Gossas, Prof. Anders Larsson, Dr. Paola Longati, Prof. Thomas Norberg, Prof. Ramesh Ramapanicker, Dr. Johan Rydberg and Prof. Lars Baltzer
Article first published online: 14 JAN 2011 | DOI: 10.1002/anie.201005059
High-affinity binders for the C-reactive protein (CRP), with dissociation constants in the pM to nM range and selectivities in human serum comparable to those of antibodies, were obtained by conjugation of 16 designed polypeptides to phosphocholine, a small molecule that binds CRP with a KD value of 5 μM (see picture). The polypeptides were not designed specifically to recognize CRP and bind by an adapted fit mechanism.