Exploring the solubility and intermolecular interactions of biologically significant amino acids l-serine and L-cysteine in binary mixtures of H2O + DMF, H2O + DMSO and H2O + ACN in temperature range from T = 288.15 K to 308.15 K

IF 3.3 3区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Biophysical chemistry Pub Date : 2024-05-27 DOI:10.1016/j.bpc.2024.107272

Jit Chakraborty , Kalachand Mahali , A.M.A. Henaish , Jahangeer Ahmed , Saad M. Alshehri , Aslam Hossain , Sanjay Roy

{"title":"Exploring the solubility and intermolecular interactions of biologically significant amino acids l-serine and L-cysteine in binary mixtures of H2O + DMF, H2O + DMSO and H2O + ACN in temperature range from T = 288.15 K to 308.15 K","authors":"Jit Chakraborty , Kalachand Mahali , A.M.A. Henaish , Jahangeer Ahmed , Saad M. Alshehri , Aslam Hossain , Sanjay Roy","doi":"10.1016/j.bpc.2024.107272","DOIUrl":null,"url":null,"abstract":"<div>In the presented work, a study on the solubility and intermolecular interactions of l-serine and L-cysteine was carried out in binary mixtures of H2O + dimethylformamide (DMF), H2O + dimethylsulfoxide (DMSO), and H2O + acetonitrile (ACN) in the temperature range of T = 288.15 K to 308.15 K. l-serine exhibited the highest solubility in water, while L-cysteine was more soluble in water-DMF. The solvation process was assessed through standard Gibbs energy calculations, indicating the solvation stability order: water-ACN > water-DMSO > water-DMF for l-serine, and water-DMF > water-DMSO > water-ACN for L-cysteine. This study also explored the influence of these amino acids on solvent–solvent interactions, revealing changes in chemical entropies and self-association patterns within the binary solvent mixtures.</div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"311 ","pages":"Article 107272"},"PeriodicalIF":3.3000,"publicationDate":"2024-05-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysical chemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0301462224001017","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

In the presented work, a study on the solubility and intermolecular interactions of l-serine and L-cysteine was carried out in binary mixtures of H₂O + dimethylformamide (DMF), H₂O + dimethylsulfoxide (DMSO), and H₂O + acetonitrile (ACN) in the temperature range of T = 288.15 K to 308.15 K. l-serine exhibited the highest solubility in water, while L-cysteine was more soluble in water-DMF. The solvation process was assessed through standard Gibbs energy calculations, indicating the solvation stability order: water-ACN > water-DMSO > water-DMF for l-serine, and water-DMF > water-DMSO > water-ACN for L-cysteine. This study also explored the influence of these amino acids on solvent–solvent interactions, revealing changes in chemical entropies and self-association patterns within the binary solvent mixtures.

Abstract Image

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

在温度范围为 T = 288.15 K 至 308.15 K 的 H2O + DMF、H2O + DMSO 和 H2O + ACN 的二元混合物中，探索具有重要生物意义的氨基酸 l-丝氨酸和 L-半胱氨酸的溶解度和分子间相互作用。

本文研究了 l-丝氨酸和 L-半胱氨酸在 H2O + 二甲基甲酰胺（DMF）、H2O + 二甲基亚砜（DMSO）和 H2O + 乙腈（ACN）的二元混合物中的溶解度和分子间相互作用，温度范围为 T = 288.15 K 至 308.15 K。通过标准吉布斯能计算对溶解过程进行了评估，结果表明溶解稳定性顺序为：l-丝氨酸为水-ACN > 水-DMSO > 水-DMF，L-半胱氨酸为水-DMF > 水-DMSO > 水-ACN。这项研究还探讨了这些氨基酸对溶剂-溶剂相互作用的影响，揭示了二元溶剂混合物中化学熵和自结合模式的变化。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Biophysical chemistry 生物-生化与分子生物学

CiteScore

6.10

自引率

10.50%

发文量

121

审稿时长

20 days

期刊介绍： Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.