人血清白蛋白在反胶束中的药物释放促进机制：结构转换的必要性。

A drug release-facilitating mechanism for human serum albumin in reverse micelles: requirement of a structural switch.

作者信息

Desfosses B, Nicot C, Waks M

机构信息

Département de Biochimie, UFR Biomédicale des Saints-Pères, Paris, France.

出版信息

Biochem Int. 1992 Feb;26(2):257-64.

PMID:1558538

Abstract

We measured the binding of a drug oxyphenylbutazone to the N-terminal peptic fragment of human serum albumin in 0.1 M Tris buffer, pH 8.0 (Kass = 2.4 10(5) M-1) and in reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate and buffer in isooctane (Kass. = 2.7 10(5) M-1). In the absence of any measured change in conformation of the fragment in reverse micelles, the peptide affinity for the drug is not decreased, in contrast to what is observed in intact albumin (HSA) under similar conditions. The interaction and the subsequent unfolding of HSA at the membrane-mimetic interface, constitutes thus a drug release-facilitating mechanism.

摘要

我们在pH值为8.0的0.1M Tris缓冲液中测定了药物羟苯基丁酮与人血清白蛋白N端消化片段的结合情况（缔合常数Kass = 2.4×10⁵ M⁻¹），并在异辛烷中双（2-乙基己基）磺基琥珀酸钠和缓冲液的反胶束中进行了测定（缔合常数Kass = 2.7×10⁵ M⁻¹）。在反胶束中该片段的构象没有任何可测变化的情况下，与在类似条件下完整白蛋白（HSA）中观察到的情况相反，该肽对药物的亲和力并未降低。因此，HSA在膜模拟界面处的相互作用及随后的展开构成了一种促进药物释放的机制。