The binding of 1,8 ANS congeners to I-FABP and comparison of some hypotheses about ANS' spectral sensitivity to environment.
The ANS congeners 1-anilinonaphthalene and 1-amino,8-sulfonato naphthalene were investigated as analogs of 1,8 anilinonaphthalene sulfonate. Like 1,8 ANS, they also bind to I-FABP, and the fully-bound spectra reveal interesting similarities and differences with respect to ANS binding. The nature of these differences suggests that certain hypotheses in the literature about ANS photophysics ought to be revised. The conceptual decomposition of energetic effects in the thermodynamics of ANS binding proposed earlier [W. Kirk, E. Kurian, F. Prendergast, Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys. J. (1996) 70 69-83.] is extended further in this report.
Kirk
William R
WR
Mayo Foundation, Rochester, Minn. 55905, USA. william.kirk@mayo.edu
D000817:Anilino Naphthalenesulfonates / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004777:Environment; D050556:Fatty Acid-Binding Proteins; D005456:Fluorescent Dyes / Q000737:chemistry* / Q000378:metabolism*; D008433:Mathematics; D011485:Protein Binding; D051381:Rats; D013050:Spectrometry, Fluorescence / Q000379:methods
D000817:Anilino Naphthalenesulfonates; D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005456:Fluorescent Dyes; C027132:1-anilino-8-naphthalenesulfonate