RAFT polymers for protein recognition

• Alan F. Tominey,
• Julia Liese,
• Sun Wei,
• Klaus Kowski,
• Thomas Schrader and
• Arno Kraft

Beilstein J. Org. Chem. 2010, 6, No. 66, doi:10.3762/bjoc.6.66

• : electrostatic interactions; hydrophobic effect; isothermal calorimetry; protein recognition; RAFT polymers; Introduction The ability of biological receptors to bind strongly and specifically to a particular molecular target is an essential part of biological machinery. The best example is the immune system

• pattern to a carboxylate, so that similar affinities would have been expected. Most likely, the difference is explained by interactions with the π-face of the tetrazolate anion, which are not possible with a carboxylate. In all cases, protein complexation by RAFT polymers was endothermic, i.e., entropy

• – admittedly much weaker – 2:1 complex. Histone association with B20CH15 is an illustrative example. The first Kd value is 16 nM, followed by very weak binding at a second site with a Kd of 1 mM. With respect to varying pI values, both RAFT polymers display little selectivity: From lysozyme (pI > 9) down to