{"title":"Interaction among bovine serum albumin (BSA) molecules in the presence of anions: a small-angle neutron scattering study","authors":"Subhankar Pandit, Sarathi Kundu, Vinod K. Aswal","doi":"10.1007/s10867-022-09608-w","DOIUrl":null,"url":null,"abstract":"<div><h2>Abstract\n</h2><div><p>Protein–protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (<i>p</i>I ≈ 4.8), is studied in the presence of anions (Cl<sup>–</sup>, Br<sup>–</sup>, I<sup>–</sup>, F<sup>–</sup>, SO<sub>4</sub><sup>2–</sup>) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the <i>p</i>I of BSA, it nearly follows the series.</p></div></div>","PeriodicalId":612,"journal":{"name":"Journal of Biological Physics","volume":null,"pages":null},"PeriodicalIF":1.8000,"publicationDate":"2022-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s10867-022-09608-w.pdf","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Biological Physics","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s10867-022-09608-w","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 1
Abstract
Abstract
Protein–protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (pI ≈ 4.8), is studied in the presence of anions (Cl–, Br–, I–, F–, SO42–) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the pI of BSA, it nearly follows the series.
期刊介绍：
Many physicists are turning their attention to domains that were not traditionally part of physics and are applying the sophisticated tools of theoretical, computational and experimental physics to investigate biological processes, systems and materials.
The Journal of Biological Physics provides a medium where this growing community of scientists can publish its results and discuss its aims and methods. It welcomes papers which use the tools of physics in an innovative way to study biological problems, as well as research aimed at providing a better understanding of the physical principles underlying biological processes.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
