河北大学学报(自然科学版) ›› 2016, Vol. 36 ›› Issue (1): 35-42.DOI: 10.3969/j.issn.1000-1565.2016.01.007

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牛血清白蛋白聚集体的分解动力学

李昊一,李冬敏,马刚,商艳丽,孙英   

  • 收稿日期:2015-09-14 出版日期:2016-01-25 发布日期:2016-01-25
  • 通讯作者: 马刚(1971—),男,北京人,河北大学教授,主要从事与蛋白质和纳米材料相关物理化学研究.E-mail:gangma@hbu.edu.cn
  • 作者简介:李昊一(1991—),女,河北廊坊人,河北大学在读硕士研究生. E-mail:haoyi19910324@sina.com.
  • 基金资助:
    国家自然科学基金资助项目(21075027);教育部科学技术研究重点项目(211014);高等学校博士学科点专项科研基金联合资助课题(20121301110003);河北省自然科学基金资助项目(B2011201082)

Structural insights into bovine serum albumin aggregates by a dissociation kinetic investigation

LI Haoyi,LI Dongmin,MA Gang,SHANG Yanli,SUN Ying   

  1. Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding 071002, China
  • Received:2015-09-14 Online:2016-01-25 Published:2016-01-25

摘要: 以牛血清白蛋白(BSA)作为模型蛋白,通过浊度法研究BSA形成的无序蛋白聚集体的分解动力学并揭示其复杂结构细节.实验发现,BSA无序聚集体在碱性条件下分解过程有4个动力学阶段,包括1个快速的分解阶段,2个相对较慢的分解阶段和1个动力学惰性阶段.由此推测BSA聚集体中至少含有4种不同的BSA单体形态.

关键词: 蛋白聚集体, 牛血清白蛋白, 浊度法, 动力学

Abstract: Protein aggregation is not only a common problem in biopharmaceutical industry involving protein drugs,but also a devastating phenomenon closely linked to numerous human diseases.Understanding structural details of protein aggregates is fundamentally important in the prediction and prevention of protein aggregation behavior.In this study,we explore to use a turbidity-based dissociation kinetic assay to tackle the complex nature of protein amorphous aggregates by a model protein,bovine serum albumin(BSA).We observe that the dissociation of BSA aggregates under basic condition consists of four distinct kinetic phases,including a burst phase,two relatively slow phases,and one kinetically inert phase.Such kinetic observation allows us to hypothesize that BSA aggregates consist of at least four different types of BSA monomeric structures at the molecular level.To the best of our knowledge,this is the first turbidity-based investigation with the aim to elucidate the structural heterogeneity of protein amorphous aggregates.

Key words: protein aggregation, bovine serum albumin, turbidity, kinetics

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