Spectral and photophysical investigations of 4＇-（p-aminophenyl）-2,2＇：6＇,2″-terpyridine （APT） have been performed in various solvents with different polarity and hydrogen-bonding ability. The emission spectra of APT are found to exhibit dual fluorescence in polar solvents, which attributes to the local excited and intramolecular charge transfer states, respectively. The two-state model is proven out for APT in polar solvent by the time-correlated single photon counting emission decay measurement. Interestingly, the linear relationships of different emission maxima and solvent polarity parameter are found for APT in protic and aprotic solvents, because of the hydrogen bond formation between APT and alcohols at the amino nitrogen N25. Furthermore, the effects of the complexation of the metal ion with tpy group of APT and the hydrogen bond formation between APT with methanol at the terpyridine nitrogen N4-NS-N14 are also presented. The appearance of new long-wave absorption and fluorescence bands indicates that a new ground state of the complexes is formed.
Agonist binding of A2A adenosine receptor （A2AAR） shows protective effects against inflammatory and immune. Efforts are exerted in understanding the general mechanism and developing A2AAR selectively binding agonists. Using molecular dynamics （MD） simula- tions, we have studied the interactions between A2AAR and its agonist （adenosine）, and analyzed the induced dynamic behaviors of the receptor. Key residues interacting with adenosine are identified： A63^2.61,I66^2.64,V84^3.32,L85^3.33,T88^3.36,F168^5.29,M177^5.38,L249^6.51,H250^6.52 and N253^6.55 interacting with adenosine with affinities larger than 0.5 kcal/mol. Moreover, no interaction between adenosine and L167^5.28 is observed, which supports our previous findings that L1675^5.28 is an antagonist specific binding reside. The dynamic be- haviors of agonist bound A2AAR are found to be different from apo-A2AAR in three typical functional switches： （i） tight ＂ionic lock＂ forms in adenosine-A2AAR, but it is in equilibrium between formation and breakage in apo-A2AAR; （ii） the ＂rotamer toggle switch＂, T88^3.36/F242^6.44/W246^6.48, adopted different rotameric conformations in adenosin-A2AAR and apo-A2AAR; （iii） adenosine-A2AAR has a flexible intracellular loop 2 （IC2） and s-helical IC3, while apo-A2AAR preferred s-helical IC2 and flexible IC3. Our results indicate that agonist binding induced different conformational rearrangements of these characteristic functional switches in adenosine-A2AAR and apo-A2AAR.
Femtosecond time-resolved fluorescence depletion spectroscopy was used in the study of the orientation relaxation of Rhodamine 700(LD700) and Oxazine 750(OX750) in DMSO. The anisotropy functions of the dye molecules were obtained from the fluorescence depletion spectra, as the polarization of probe pulse is parallel and perpendicular respectively. The results show that the transition dipole moment of the pump and the probe of LD700 and OX750 are parallel. The time constants of the orientation relaxation of these dye molecules in DMSO are 1.8 and 1.9 ps for LD700 and OX750, respectively.
