Biophysics Section, Blackett Laboratory, Imperial College, United Kingdom.
Drug Metab Pharmacokinet. 2009;24(4):342-57. doi: 10.2133/dmpk.24.342.
Human serum albumin (HSA) is an abundant and highly soluble plasma protein with the capacity to bind a remarkably diverse set of lipophilic anionic compounds so that it fulfils important roles in the transport of nutrients, hormones and toxins. The protein attracts great interest from the pharmaceutical industry since it can also bind a variety of drug molecules, impacting their delivery and efficacy. Our understanding of the binding and transport properties of albumin has been transformed by structural studies of the protein, in which crystallographic analysis has played a leading role. This review summarises the main insights to have accrued from this work, highlighting the significant advances that have been made but also pointing out some of the challenges ahead. Since further progress is likely to benefit from increased structural scrutiny of HSA, methodological developments instrumental to the success of crystallographic analysis of the protein are discussed in some detail.
人血清白蛋白（HSA）是一种丰富且高度可溶性的血浆蛋白，具有结合一系列显著不同的亲脂性阴离子化合物的能力，从而在营养物质、激素和毒素的运输中发挥重要作用。由于 HSA 还可以结合各种药物分子，影响其递送和疗效，因此该蛋白引起了制药行业的极大兴趣。结构研究改变了我们对白蛋白结合和运输特性的理解，其中晶体学分析发挥了主导作用。这篇综述总结了从这项工作中获得的主要见解，强调了取得的重大进展，但也指出了未来的一些挑战。由于进一步的进展可能受益于对 HSA 进行更深入的结构研究，因此详细讨论了对 HSA 进行晶体学分析取得成功的方法学进展。
