Entropy driven binding

A. Miklavc, D. Kocjan, J. Mavri, J. Roller and D. Hadzi, On the fundamental difference in thermodynamics of agonist and antagonist interactions with P-adrenergic receptors and the mechanism of entropy-driven binding. Biochem. Pharmacol., 40 (1990) 663-669. 

The interaction between 4-(4-hydroxybut-2-ynyloxy)-3-(phenylsulfonyl)-l,2,5-oxadiazole-2-oxide 16 and bovine serum albumin (BSA) was studied by spectroscopic methods including fluorescence and UV-Vis absorption spectroscopy. The results indicate that molecules 16 bind with BSA forming 1 1 complex. Thermodynamic parameters, such as AH, AG, and A.Y, were calculated. The results indicate that the binding reaction is mainly entropy driven and hydrophobic forces play a major role in this reaction <2006CHJ1050>. 

Analysis of thermodynamical parameters of LGICR have revealed that five out of six receptors are thermodynamically discriminated (Table 2.5, Fig. 2.3b). As for the glycine receptor, the agonist binding has to be classified as entropy-driven (2 < AH0... 

---