Protein surface recognition by synthetic receptors based on a tetraphenylporphyrin scaffold.
[structure: see text] Receptors based on a tetraphenylporphyrin scaffold bearing different charged and hydrophobic groups have been synthesized. The interactions of these with horse heart cytochrome c were studied by fluorescence spectroscopy. Receptor 4 was identified to be the strongest synthetic receptor (K(d) = 20 nM) for cytochrome c. The differences in affinity among the receptors reflected a dependence on the number of anionic and hydrophobic groups.
Jain
R K
RK
Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
Hamilton
A D
AD
D000818:Animals; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism*; D018716:Molecular Mimicry; D011166:Porphyrins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D003574:Cytochrome c Group; D011166:Porphyrins; C409084:tetraphenylporphyrin