Dalla Via L, Di Noto V, Toninello A
Università di Padova, Centro di Studio delle Biomembrane del CNR di Padova, viale G. Colombo 3, Padova, 35121, Italy.
Arch Biochem Biophys. 1999 May 15;365(2):231-8. doi: 10.1006/abbi.1999.1170.
The binding of spermidine and putrescine to mitochondrial membranes was studied by applying a thermodynamic model of ligand-receptor interactions developed both for equilibrium and far-from-equilibrium binding processes (V. Di Noto, L. Dalla Via, A. Toninello, and M. Vidali Macromol. Theory Simul. 5, 165-181, 1996). Results demonstrate the presence of two monocoordinated binding sites (S1 and S2) for spermidine and one monocoordinated binding site (S2) for putrescine, all exhibiting high capacity and low affinity. It is proposed that differences in the polyamines' flexibility and hydrophilicity perhaps contributes to the observed variations in their interactions with the two sites. A comparison of the binding parameters of these polyamines with those of spermine reveals differences in the specific function of the S1 and S2 sites, identified in studies of spermine binding (L. Dalla Via, V. Di Noto, D. Siliprandi, and A. Toninello Biochim. Biophys. Acta 1284, 247-252, 1996).
通过应用一种针对平衡和远离平衡结合过程开发的配体 - 受体相互作用热力学模型（V. 迪诺托、L. 达拉·维亚、A. 托尼内洛和 M. 维达利，《大分子理论与模拟》5，165 - 181，1996年），研究了亚精胺和腐胺与线粒体膜的结合。结果表明，亚精胺存在两个单配位结合位点（S1和S2），腐胺存在一个单配位结合位点（S2），所有这些位点都表现出高容量和低亲和力。有人提出，多胺的柔韧性和亲水性差异可能导致了它们与这两个位点相互作用的观察到的变化。将这些多胺的结合参数与精胺的结合参数进行比较，揭示了在精胺结合研究中确定的S1和S2位点的特定功能差异（L. 达拉·维亚、V. 迪诺托、D. 西利普兰迪和A. 托尼内洛，《生物化学与生物物理学报》1284，247 - 252，1996年）。
