| 引用本文: | 陆会宁,齐燕姣,冯树华,李世玺,赵娅敏,金能智.血清白蛋白序列中的相似氨基酸突变特点分析[J].生物信息学,2015,13(3):179-185. |
| LU Huining,QI Yanjiao,FENG Shuhua,LI Shixi,ZHAO Yamin,JIN Nengzhi.Mutational characteristics analysis of the similar amino acid of serum albumin sequences[J].Chinese Journal of Bioinformatics,2015,13(3):179-185. |
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| 血清白蛋白序列中的相似氨基酸突变特点分析 |
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陆会宁1, 齐燕姣2, 冯树华2,李世玺2, 赵娅敏2,金能智3
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(1. 西北民族大学生命科学与工程学院, 兰州 730124;2. 西北民族大学化工学院, 兰州 730124;3. 甘肃省计算中心,兰州 730000)
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| 摘要: |
| 血清白蛋白是必不可少的生命物质,在生命运动和发展延续中起着重要的作用。它不仅能维持正常的血浆渗透压,最重要的是能够储存和运输众多的内源性和外源性物质。本文利用生物信息学的方法分析了几种不同物种的血清白蛋白的结构信息和疏水性特点,研究表明人、牛、猴、兔、狼、猫的血清白蛋白序列均属于亲水性蛋白质,在100 bp以内的疏水性值差别比较明显。通过对血清白蛋白进行多序列比对分析,发现兔血清白蛋白的氨基酸突变的数目是最多的。在这几种血清白蛋白序列中,氨基酸突变更容易发生在结构相似、极性相似和能量比较接近的氨基酸之间,如D和L、E和D。对于人血清白蛋白来说,从疏水性的丙氨酸A到酸性的谷氨酸E的突变比较多,使得人血清白蛋白在进化过程中的亲水性增强,是个很好的储存和运输小分子的载体。这些基于生物信息学方面的血清白蛋白的突变及其进化关系的研究,为进一步研究药物与血清白蛋白的相互作用在其他物种中表现和特点提供了良好的基础。 |
| 关键词: 血清白蛋白 序列比对 突变 疏水性 |
| DOI：10.3969/j.issn.1672-5565.2015.03.06 |
| 分类号:Q-03 |
| 基金项目: |
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| Mutational characteristics analysis of the similar amino acid of serum albumin sequences |
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LU Huining1, QI Yanjiao 2, FENG Shuhua2, LI Shixi2,ZHAO Yamin2, JIN Nengzhi3
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(1. Department of Life Sciences and Biological Engineering, Northwest University for Nationalities, Lanzhou 730124, China;2. Department of Chemical Engineering, Northwest University for Nationalities, Lanzhou 730124, China;3. Gansu Province Computing Center, Lanzhou 730000, China)
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| Abstract: |
| Serum albumin is essential to life and plays an important role in the life movement and development. It can not only maintain normal plasma osmolality, but also can store and transport many endogenous and exogenous substances. In this paper, the structure information and hydrophobic characteristics of serum albumins from several different species were analyzed by using bioinformatics. Results indicated that serum albumin sequences from different species were all hydrophilic, such as Homo sapiens, Bos Taurus, Rabbit, Felis catus, Macaca mulatta and Canis lupushuman. Hydrophobic value was relatively obvious within 100 bp of these serum albumin sequences. By using multiple sequence alignment analysis, we found that the rabbit had the most number of amino acid mutations. Among these serum albumin sequences, the amino acid mutations were more likely to occur between amino acid with similar structure, similar hydrophilic and energy, such as D and L, E and D. For the human serum albumin, mutations from hydrophobic alanine A to glutamic E were relatively much more than others, which may be related with its good hydrophily and carrier of preserving or transporting small molecules. The analysis of mutation and evolutionary relationships based on bioinformatics could provide good foundation for further studying the interaction between drugs and serum albumin sequences in other species. |
| Key words: Serum albumin Sequence alignment Mutation Hydrophobic |
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