Mass spectrometric determination of association constants of bovine serum albumin (BSA) with para-sulphonato-calix[n]arene derivatives

被引：30

作者：

Da Silva, E ^{[1
]}

Rousseau, CF ^{[1
]}

Zanella-Cléon, I ^{[1
]}

Becchi, M ^{[1
]}

Coleman, AW ^{[1
]}

机构：

[1] CNRS, Inst Biol & Chim Prot, UMR 5086, F-69367 Lyon, France

来源：

JOURNAL OF INCLUSION PHENOMENA AND MACROCYCLIC CHEMISTRY | 2006年 / 54卷 / 1-2期

关键词：

binding constants; bovine serum albumin; calixarene; electrospray mass spectrometry; selective interactions;

D O I：

10.1007/s10847-005-3995-2

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Electrospray Ionization Mass Spectrometry (ESI/MS) has been used to determine the association constants (K-As) and binding stoichiometries for parent para-Sulphonato-calix[n]arenes and their derivatives with bovine serum albumin (BSA). K-A values were determined by titration experiments using a constant concentration of protein. K-A measurements were carried out in a methanol-formic acid solution. 5,11,17,23-tetra-Sulphonato-calix[4]arene (1a) and 25-mono-(2-aminoethoxy)-5,11,17,23-tetra-Sulphonato-calix[4]arene (1d) interact strongly with BSA showing 3 non-equivalent binding sites with K-A1 = 7.69 x 10(5) M-1, K-A2 = 3.85 x 10(5) M-1, K-A3 = 0.33 x 10(5) M-1 and K-A1 = 1.69 x10(5) M-1, K-A2 = 2.94 x 10(5) M-1, K-A3 = 0.60 x10(5) M-1, respectively. The strength of the interactions between the calixarene and BSA is inversely proportional to the size of macrocyclic ring: n = 4 > n=6 >> n=8.

引用

页码：53 / 59

页数：7