{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,17]],"date-time":"2026-01-17T07:23:38Z","timestamp":1768634618962,"version":"3.49.0"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,8,17]],"date-time":"2022-08-17T00:00:00Z","timestamp":1660694400000},"content-version":"am","delay-in-days":320,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["19K22377"],"award-info":[{"award-number":["19K22377"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2021,10]]},"DOI":"10.1016\/j.ijbiomac.2021.08.070","type":"journal-article","created":{"date-parts":[[2021,8,13]],"date-time":"2021-08-13T18:16:45Z","timestamp":1628878605000},"page":"670-677","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["Insight into the protein salting-in mechanism of arginine, magnesium chloride and ethylene glycol: Solvent interaction with aromatic solutes"],"prefix":"10.1016","volume":"188","author":[{"given":"Tomoto","family":"Ura","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tsutomu","family":"Arakawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kentaro","family":"Shiraki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0005","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1007\/BF01918191","article-title":"Zur lehre von der wirkung der salze","volume":"24","author":"Hofmeister","year":"1888","journal-title":"Arch. Expt. Pathol. Pharmakol."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0010","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1016\/S0006-3495(96)79404-3","article-title":"How hofimeister ion interactions affect protein stability","volume":"71","author":"Baldwin","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0015","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1016\/S0021-9258(18)93609-4","article-title":"Reversible denaturation of ribonuclease in aqueous solutions as influenced by polyhydric alcohols and some other additives","volume":"243","author":"Gerlsma","year":"1968","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0020","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1111\/j.1432-1033.1970.tb00272.x","article-title":"The effects of polyhydric and monohydric alcohols on the heat induced reversible denaturation of chymotrypsinogen a","volume":"14","author":"Gerlsma","year":"1970","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0025","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1111\/j.1399-3011.1972.tb03444.x","article-title":"The effect of polyhydric and monohydric alcohols on the heat-induced reversible denaturation of lysozyme and ribonuclease","volume":"4","author":"Gerlsma","year":"1972","journal-title":"Int. J. Peptide Protein Res."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0030","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1111\/j.1399-3011.1974.tb02362.x","article-title":"The effects of combining two different alcohols on the heat-induced reversible denaturation of ribonuclease","volume":"6","author":"Gerlsma","year":"1974","journal-title":"Int. J. Peptide Protein Res."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0035","doi-asserted-by":"crossref","first-page":"4677","DOI":"10.1021\/bi00519a024","article-title":"Thermodynamic and kinetic examination of protein stabilization by glycerol","volume":"20","author":"Gekko","year":"1981","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0040","doi-asserted-by":"crossref","first-page":"4667","DOI":"10.1021\/bi00519a023","article-title":"Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures","volume":"20","author":"Gekko","year":"1981","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0045","doi-asserted-by":"crossref","first-page":"7193","DOI":"10.1016\/S0021-9258(19)68947-7","article-title":"The stabilization of proteins by sucrose","volume":"256","author":"Lee","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0050","doi-asserted-by":"crossref","first-page":"6536","DOI":"10.1021\/bi00268a033","article-title":"Stabilization of protein structure by sugars","volume":"21","author":"Arakawa","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0055","doi-asserted-by":"crossref","first-page":"4076","DOI":"10.1016\/S0021-9258(18)51830-5","article-title":"The solubility of amino acids and related compounds in aqueous urea solutions","volume":"238","author":"Nozaki","year":"1963","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0060","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1016\/S0021-9258(19)77141-5","article-title":"The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions","volume":"245","author":"Nozaki","year":"1970","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0065","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1021\/bi00699a005","article-title":"Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride","volume":"13","author":"Lee","year":"1974","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0070","doi-asserted-by":"crossref","first-page":"6545","DOI":"10.1021\/bi00268a034","article-title":"Preferential interactions of proteins with salts in concentrated solutions","volume":"21","author":"Arakawa","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0075","doi-asserted-by":"crossref","first-page":"5912","DOI":"10.1021\/bi00320a004","article-title":"Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding","volume":"23","author":"Arakawa","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0080","doi-asserted-by":"crossref","first-page":"5924","DOI":"10.1021\/bi00320a005","article-title":"Protein stabilization and destabilization by guanidinium salts","volume":"23","author":"Arakawa","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0085","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1021\/bi00459a036","article-title":"Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system","volume":"29","author":"Arakawa","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0090","doi-asserted-by":"crossref","first-page":"1924","DOI":"10.1021\/bi00459a037","article-title":"Why preferential hydration does not always stabilize the native structure of globular proteins","volume":"29","author":"Arakawa","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0095","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/0003-9861(77)90434-9","article-title":"Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series","volume":"183","author":"Melander","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0100","first-page":"343","article-title":"Equilibrium of heterogeneous substances","volume":"3","author":"Gibbs","year":"1878","journal-title":"Trans. Conn. Acad. Arts Sci."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0105","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1021\/j150113a003","article-title":"The attraction pressure","volume":"14","author":"Traube","year":"1910","journal-title":"J. Phys. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0110","doi-asserted-by":"crossref","first-page":"408","DOI":"10.2174\/138920109788488851","article-title":"Suppression of protein aggregation by L-arginine","volume":"10","author":"Lange","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0115","doi-asserted-by":"crossref","first-page":"921","DOI":"10.2174\/092986606778256171","article-title":"Aggregation suppression of proteins by arginine during thermal unfolding","volume":"13","author":"Arakawa","year":"2006","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0120","doi-asserted-by":"crossref","first-page":"13426","DOI":"10.1021\/jp108399g","article-title":"Interactions of arginine with proteins and the mechanism by which it inhibits aggregation","volume":"114","author":"Shukla","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0125","doi-asserted-by":"crossref","first-page":"15178","DOI":"10.1021\/bi00254a029","article-title":"Contribution of the surface free energy perturbation to protein-solvent interactions","volume":"33","author":"Kita","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bpc.2006.12.007","article-title":"Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects","volume":"127","author":"Arakawa","year":"2007","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0135","doi-asserted-by":"crossref","first-page":"13426","DOI":"10.1021\/jp108399g","article-title":"Interactions of arginine with proteins and the mechanism by which it inhibits aggregation","volume":"114","author":"Shukla","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0140","doi-asserted-by":"crossref","first-page":"7447","DOI":"10.1021\/jp111920y","article-title":"Arginine and the hofmeister series: the role of ion-ion interactions in protein aggregation suppression","volume":"115","author":"Schneider","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0145","doi-asserted-by":"crossref","first-page":"15065","DOI":"10.1073\/pnas.0507053102","article-title":"Predicting the energetics of osmolyte-induced protein folding\/unfolding","volume":"102","author":"Auton","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0150","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0076-6879(07)28023-1","article-title":"Application of the transfer model to understand how naturally occurring osmolytes affect protein stability","volume":"428","author":"Auton","year":"2007","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0155","doi-asserted-by":"crossref","first-page":"2211","DOI":"10.1016\/S0021-9258(19)77210-X","article-title":"The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. establishment of a hydrophobicity scale","volume":"246","author":"Nozaki","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0160","doi-asserted-by":"crossref","first-page":"3568","DOI":"10.1016\/S0021-9258(18)97181-4","article-title":"The solubility of amino acids and related compounds in ethylene glycol solutions","volume":"240","author":"Nozaki","year":"1965","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0165","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1039\/c2pp05341a","article-title":"Pi-cation interactions as the origin of the weak absorption at 532 nm observed in tryptophan-containing polypeptides","volume":"11","author":"Roveri","year":"2012","journal-title":"Photochem. Photobiol. Sci."},{"issue":"4","key":"10.1016\/j.ijbiomac.2021.08.070_bb0170","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1093\/jb\/mvr004","article-title":"Arginine increases the solubility of alkyl gallates through interaction with the aromatic ring","volume":"149","author":"Ariki","year":"2011","journal-title":"J. Biochem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0175","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1006\/jmbi.2000.4033","article-title":"Stabilization of bound polycyclic aromatic hydrocarbons by a pi-cation interaction","volume":"302","author":"Pellequer","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0180","doi-asserted-by":"crossref","first-page":"27105","DOI":"10.1039\/D0CP03707A","article-title":"The phenoxyl group-modulated interplay of cation-p and s-type interactions in the alkali metal series","volume":"22","author":"Prampolini","year":"2020","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0185","doi-asserted-by":"crossref","first-page":"3155","DOI":"10.1002\/jps.20976","article-title":"Antimicrobial preservative use in parenteral products: past and present","volume":"96","author":"Meyer","year":"2007","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0190","doi-asserted-by":"crossref","unstructured":"J.J. Lucchini J. Crowe A Cremieux Antibacterial activity of phenolic compounds and aromatic alcohols Res. Microbiol. 141 199 499 510.","DOI":"10.1016\/0923-2508(90)90075-2"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0195","doi-asserted-by":"crossref","first-page":"2470","DOI":"10.1021\/ja01089a029","article-title":"The effect of concentrated salt solutions on the activity coefficient of acetyltetraglycine ethyl ester","volume":"87","author":"Robinson","year":"1965","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0200","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1021\/acsanm.0c03047","article-title":"Aromaphilicity index of amino acids: molecular dynamics simulations of the protein binding affinity for carbon nanomaterials","volume":"4","author":"Hirano","year":"2021","journal-title":"ACS Appl. Nano Mater."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0205","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.bpc.2007.09.004","article-title":"Protein precipitation and denaturation by dimethyl sulfoxide","volume":"131","author":"Arakawa","year":"2007","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0210","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.31486","article-title":"pi-pi contacts are an overlooked protein feature relavant to phase separation","volume":"7","author":"Vernon","year":"2018","journal-title":"elife"},{"issue":"1","key":"10.1016\/j.ijbiomac.2021.08.070_bb0215","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1021\/acs.molpharmaceut.0c00905","article-title":"Adenosine triphosphate-induced rapid Liquid-Liquid phase separation of a model IgG1 mAb","volume":"18","author":"Tian","year":"2021","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0220","doi-asserted-by":"crossref","DOI":"10.1016\/j.xcrp.2021.100343","article-title":"Hofmeister versus neuberg: is ATP really a biological hydrotrope?","volume":"2","author":"Mehringer","year":"2021","journal-title":"Cell Reports Physical Science"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0225","first-page":"598","article-title":"ATP-induced noncooperative thermal unfolding of hen lysozyme","volume":"397","author":"Liu","year":"2010","journal-title":"Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0230","doi-asserted-by":"crossref","first-page":"5525","DOI":"10.1021\/ja00170a016","article-title":"The nature of p-p interactions","volume":"112","author":"Hunter","year":"1990","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0235","doi-asserted-by":"crossref","first-page":"3116","DOI":"10.1002\/cphc.201100542","article-title":"Wheeler. substituent effects on non-covalent interactions with aromatic rings: insights from computational chemistry","volume":"12","author":"Raju","year":"2011","journal-title":"ChemPhysChem"},{"key":"10.1016\/j.ijbiomac.2021.08.070_bb0240","doi-asserted-by":"crossref","first-page":"3126","DOI":"10.1021\/ja809097r","article-title":"Substituenteffects in cation\/p interactions and electrostatic potentials above the centers of substituted benzenes are due primarily to through-space effects of the substituents","volume":"131","author":"Wheeler","year":"2009","journal-title":"J. Am. Chem. Soc."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813021017293?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813021017293?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,2]],"date-time":"2025-09-02T04:48:24Z","timestamp":1756788504000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813021017293"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,10]]},"references-count":48,"alternative-id":["S0141813021017293"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2021.08.070","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2021,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Insight into the protein salting-in mechanism of arginine, magnesium chloride and ethylene glycol: Solvent interaction with aromatic solutes","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2021.08.070","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}