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Powerful Protein Binders from Designed Polypeptides and Small Organic Molecules—A General Concept for Protein Recognition
Author(s) -
Tegler Lotta T.,
glaton Guillaume,
Büttner Frank,
Caldwell Karin,
Christopeit Tony,
Danielson U. Helena,
Fromell Karin,
Gossas Thomas,
Larsson Anders,
Longati Paola,
Norberg Thomas,
Ramapanicker Ramesh,
Rydberg Johan,
Baltzer Lars
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201005059
Subject(s) - dissociation constant , dissociation (chemistry) , organic molecules , phosphocholine , combinatorial chemistry , small molecule , chemistry , molecule , computational biology , biochemistry , computer science , biophysics , nanotechnology , materials science , biology , organic chemistry , receptor , phospholipid , membrane , phosphatidylcholine
High‐affinity binders for the C‐reactive protein (CRP), with dissociation constants in the p M to n M 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 K D value of 5 μ M (see picture). The polypeptides were not designed specifically to recognize CRP and bind by an adapted fit mechanism.