{"title":"胍盐中的离子配对倾向决定其蛋白质(去)稳定行为","authors":"Ria Saha, Subhadip Chakraborty, Krishnendu Sinha, Partha Pyne, Sreya Pal, Anjan Barman, Suman Chakrabarty and Rajib Kumar Mitra*, ","doi":"10.1021/acs.jpclett.4c0164610.1021/acs.jpclett.4c01646","DOIUrl":null,"url":null,"abstract":"<p >Since the proposition of the Hofmeister series, guanidinium (Gdm) salts hold a special mention in protein science owing to their contrasting effect on protein(s) depending on the counteranion(s). For example, while GdmCl is known to act as a potential protein denaturant, Gdm<sub>2</sub>SO<sub>4</sub> offers minimal effect on protein structure. Despite the fact that theoretical studies reckon the formation of ion-pairing to be responsible for such behavior, experimental validation of this hypothesis is still in sparse. In this study, we combine electrochemical impedance spectroscopy (EIS) and THz spectroscopy to underline the effect of GdmCl and Gdm<sub>2</sub>SO<sub>4</sub> on a model amide molecule <i>N</i>-methylacetamide (NMA). Molecular dynamics (MD) simulation studies predict that Gdm<sub>2</sub>SO<sub>4</sub> forms heteroion pairing in water, which inhibits Gdm<sup>+</sup> ions to approach NMA molecules, while in case of GdmCl, Gdm<sup>+</sup> ions directly interact with NMA. The experimental findings on ion hydration, specifically the detailed analysis of the ion–water rattling mode, which appears in the THz frequency domain, unambiguously endorse this hypothesis. Our study establishes the fact that the propensity of ion-pairing in Gdm salts dictates their (de)stabilization effect on proteins.</p>","PeriodicalId":62,"journal":{"name":"The Journal of Physical Chemistry Letters","volume":null,"pages":null},"PeriodicalIF":4.8000,"publicationDate":"2024-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Ion-Pairing Propensity in Guanidinium Salts Dictates Their Protein (De)stabilization Behavior\",\"authors\":\"Ria Saha, Subhadip Chakraborty, Krishnendu Sinha, Partha Pyne, Sreya Pal, Anjan Barman, Suman Chakrabarty and Rajib Kumar Mitra*, \",\"doi\":\"10.1021/acs.jpclett.4c0164610.1021/acs.jpclett.4c01646\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Since the proposition of the Hofmeister series, guanidinium (Gdm) salts hold a special mention in protein science owing to their contrasting effect on protein(s) depending on the counteranion(s). For example, while GdmCl is known to act as a potential protein denaturant, Gdm<sub>2</sub>SO<sub>4</sub> offers minimal effect on protein structure. Despite the fact that theoretical studies reckon the formation of ion-pairing to be responsible for such behavior, experimental validation of this hypothesis is still in sparse. In this study, we combine electrochemical impedance spectroscopy (EIS) and THz spectroscopy to underline the effect of GdmCl and Gdm<sub>2</sub>SO<sub>4</sub> on a model amide molecule <i>N</i>-methylacetamide (NMA). Molecular dynamics (MD) simulation studies predict that Gdm<sub>2</sub>SO<sub>4</sub> forms heteroion pairing in water, which inhibits Gdm<sup>+</sup> ions to approach NMA molecules, while in case of GdmCl, Gdm<sup>+</sup> ions directly interact with NMA. The experimental findings on ion hydration, specifically the detailed analysis of the ion–water rattling mode, which appears in the THz frequency domain, unambiguously endorse this hypothesis. Our study establishes the fact that the propensity of ion-pairing in Gdm salts dictates their (de)stabilization effect on proteins.</p>\",\"PeriodicalId\":62,\"journal\":{\"name\":\"The Journal of Physical Chemistry Letters\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2024-10-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Physical Chemistry Letters\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.jpclett.4c01646\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Physical Chemistry Letters","FirstCategoryId":"1","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.jpclett.4c01646","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Ion-Pairing Propensity in Guanidinium Salts Dictates Their Protein (De)stabilization Behavior
Since the proposition of the Hofmeister series, guanidinium (Gdm) salts hold a special mention in protein science owing to their contrasting effect on protein(s) depending on the counteranion(s). For example, while GdmCl is known to act as a potential protein denaturant, Gdm2SO4 offers minimal effect on protein structure. Despite the fact that theoretical studies reckon the formation of ion-pairing to be responsible for such behavior, experimental validation of this hypothesis is still in sparse. In this study, we combine electrochemical impedance spectroscopy (EIS) and THz spectroscopy to underline the effect of GdmCl and Gdm2SO4 on a model amide molecule N-methylacetamide (NMA). Molecular dynamics (MD) simulation studies predict that Gdm2SO4 forms heteroion pairing in water, which inhibits Gdm+ ions to approach NMA molecules, while in case of GdmCl, Gdm+ ions directly interact with NMA. The experimental findings on ion hydration, specifically the detailed analysis of the ion–water rattling mode, which appears in the THz frequency domain, unambiguously endorse this hypothesis. Our study establishes the fact that the propensity of ion-pairing in Gdm salts dictates their (de)stabilization effect on proteins.
期刊介绍:
The Journal of Physical Chemistry (JPC) Letters is devoted to reporting new and original experimental and theoretical basic research of interest to physical chemists, biophysical chemists, chemical physicists, physicists, material scientists, and engineers. An important criterion for acceptance is that the paper reports a significant scientific advance and/or physical insight such that rapid publication is essential. Two issues of JPC Letters are published each month.