生物信息学
生物信息學
생물신식학
China Journal of Bioinformatics
2015年
3期
179-185
,共7页
陆会宁%齐燕姣%冯树华%李世玺%赵娅敏%金能智
陸會寧%齊燕姣%馮樹華%李世璽%趙婭敏%金能智
륙회저%제연교%풍수화%리세새%조아민%금능지
血清白蛋白%序列比对%突变%疏水性
血清白蛋白%序列比對%突變%疏水性
혈청백단백%서렬비대%돌변%소수성
Serum albumin%Sequence alignment%Mutation%Hydrophobic
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.
血清白蛋白是必不可少的生命物質,在生命運動和髮展延續中起著重要的作用. 它不僅能維持正常的血漿滲透壓,最重要的是能夠儲存和運輸衆多的內源性和外源性物質. 本文利用生物信息學的方法分析瞭幾種不同物種的血清白蛋白的結構信息和疏水性特點,研究錶明人、牛、猴、兔、狼、貓的血清白蛋白序列均屬于親水性蛋白質,在100 bp以內的疏水性值差彆比較明顯. 通過對血清白蛋白進行多序列比對分析,髮現兔血清白蛋白的氨基痠突變的數目是最多的. 在這幾種血清白蛋白序列中,氨基痠突變更容易髮生在結構相似、極性相似和能量比較接近的氨基痠之間,如D和L、E和D. 對于人血清白蛋白來說,從疏水性的丙氨痠A到痠性的穀氨痠E的突變比較多,使得人血清白蛋白在進化過程中的親水性增彊,是箇很好的儲存和運輸小分子的載體. 這些基于生物信息學方麵的血清白蛋白的突變及其進化關繫的研究,為進一步研究藥物與血清白蛋白的相互作用在其他物種中錶現和特點提供瞭良好的基礎.
혈청백단백시필불가소적생명물질,재생명운동화발전연속중기착중요적작용. 타불부능유지정상적혈장삼투압,최중요적시능구저존화운수음다적내원성화외원성물질. 본문이용생물신식학적방법분석료궤충불동물충적혈청백단백적결구신식화소수성특점,연구표명인、우、후、토、랑、묘적혈청백단백서렬균속우친수성단백질,재100 bp이내적소수성치차별비교명현. 통과대혈청백단백진행다서렬비대분석,발현토혈청백단백적안기산돌변적수목시최다적. 재저궤충혈청백단백서렬중,안기산돌변경용역발생재결구상사、겁성상사화능량비교접근적안기산지간,여D화L、E화D. 대우인혈청백단백래설,종소수성적병안산A도산성적곡안산E적돌변비교다,사득인혈청백단백재진화과정중적친수성증강,시개흔호적저존화운수소분자적재체. 저사기우생물신식학방면적혈청백단백적돌변급기진화관계적연구,위진일보연구약물여혈청백단백적상호작용재기타물충중표현화특점제공료량호적기출.
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.