{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T13:15:40Z","timestamp":1779282940077,"version":"3.51.4"},"reference-count":70,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2027,1,27]],"date-time":"2027-01-27T00:00:00Z","timestamp":1801008000000},"content-version":"am","delay-in-days":271,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100004334","name":"Merck & Co Inc","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100004334","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Colloid and Interface Science"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1016\/j.jcis.2026.139940","type":"journal-article","created":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T15:53:31Z","timestamp":1769010811000},"page":"139940","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Effects of arginine on the interfacial behavior of proteins"],"prefix":"10.1016","volume":"709","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1922-8545","authenticated-orcid":false,"given":"Peyman","family":"Dastyar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0730-6104","authenticated-orcid":false,"given":"Harsa","family":"Mitra","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-6842-651X","authenticated-orcid":false,"given":"Caitlin V.","family":"Wood","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1322-759X","authenticated-orcid":false,"given":"Thomas A.","family":"Everett","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0655-9580","authenticated-orcid":false,"given":"Yu-Jiun","family":"Lin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2570-1631","authenticated-orcid":false,"given":"Yu","family":"Tian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3301-3193","authenticated-orcid":false,"given":"Arezoo M.","family":"Ardekani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"8","key":"10.1016\/j.jcis.2026.139940_bib0001","doi-asserted-by":"crossref","first-page":"9977","DOI":"10.1021\/acsami.9b21979","article-title":"Armoring the interface with surfactants to prevent the adsorption of monoclonal antibodies","volume":"12","author":"Kanthe","year":"2020","journal-title":"ACS Appl. Mater. Interf."},{"key":"10.1016\/j.jcis.2026.139940_bib0002","first-page":"630","volume":"34","author":"Kannan","year":"2018","journal-title":"Monoclonal Antibody Interfaces"},{"key":"10.1016\/j.jcis.2026.139940_bib0003","series-title":"Adsorption of polysorbate 20 and proteins on hydrophobic polystyrene surfaces studied by neutron reflectometry","first-page":"94","author":"Zhang","year":"2018"},{"issue":"10","key":"10.1016\/j.jcis.2026.139940_bib0004","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1016\/j.addr.2012.09.039","article-title":"Fusion protein linkers: property, design and functionality","volume":"65","author":"Chen","year":"2013","journal-title":"Adv. Drug Deliv. Rev."},{"issue":"5","key":"10.1016\/j.jcis.2026.139940_bib0005","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1177\/0091270004273321","article-title":"Clinical pharmacokinetics of etanercept: a fully humanized soluble recombinant tumor necrosis factor receptor fusion protein","volume":"45","author":"Zhou","year":"2005","journal-title":"J. Clin. Pharmacol."},{"issue":"5","key":"10.1016\/j.jcis.2026.139940_bib0006","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1517\/14712598.2014.896334","article-title":"Etanercept-tnf receptor and IgG1 fc fusion protein: is it different from other tnf blockers?","volume":"14","author":"Marotte","year":"2014","journal-title":"Expert. Opin. Biol. Ther."},{"key":"10.1016\/j.jcis.2026.139940_bib0007","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jim.2017.03.007","article-title":"Establishment of the first WHO international standard for etanercept, a tnf receptor ii fc fusion protein: report of an international collaborative study","volume":"447","author":"Wadhwa","year":"2017","journal-title":"J. Immunol. Methods"},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0008","first-page":"284","article-title":"Fusion-proteins as biopharmaceuticals-applications and challenges, current opinion in drug","volume":"12","author":"Schmidt","year":"2009","journal-title":"Disc. Develop."},{"issue":"4","key":"10.1016\/j.jcis.2026.139940_bib0009","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1056\/NEJM199901283400401","article-title":"A trial of etanercept, a recombinant tumor necrosis factor receptor: Fc fusion protein, in patients with rheumatoid arthritis receiving methotrexate","volume":"340","author":"Weinblatt","year":"1999","journal-title":"N Engl. J. Med."},{"key":"10.1016\/j.jcis.2026.139940_bib0010","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.ejpb.2016.07.020","article-title":"Reversible NaCl-induced aggregation of a monoclonal antibody at low ph: characterization of aggregates and factors affecting aggregation","volume":"107","author":"Bickel","year":"2016","journal-title":"Eur. J. Pharm. Biopharm."},{"issue":"10","key":"10.1016\/j.jcis.2026.139940_bib0011","doi-asserted-by":"crossref","first-page":"4319","DOI":"10.1021\/acs.molpharmaceut.9b00687","article-title":"Studying excipient modulated physical stability and viscosity of monoclonal antibody formulations using small-angle scattering","volume":"16","author":"Xu","year":"2019","journal-title":"Mol. Pharm."},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0012","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1002\/prot.20417","article-title":"Cation-\u03c0 interactions in protein-protein interfaces","volume":"59","author":"Crowley","year":"2005","journal-title":"Proteins Struct. Funct. Bioinf."},{"key":"10.1016\/j.jcis.2026.139940_bib0013","series-title":"Biological importance of arginine: a comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins","first-page":"128646","author":"Gupta","year":"2023"},{"key":"10.1016\/j.jcis.2026.139940_bib0014","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.128646","article-title":"Biological importance of arginine: a comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins","volume":"257","author":"Gupta","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"issue":"1","key":"10.1016\/j.jcis.2026.139940_bib0015","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pep.2005.03.028","article-title":"Is arginine a protein-denaturant?","volume":"42","author":"Ishibashi","year":"2005","journal-title":"Protein Expr. Purif."},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0016","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/j.ijpharm.2014.12.038","article-title":"Preferential interactions between protein and arginine: effects of arginine on tertiary conformational and colloidal stability of protein solution","volume":"478","author":"Wen","year":"2015","journal-title":"Int. J. Pharm."},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0017","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1111\/ijfs.14752","article-title":"Manipulating interfacial behaviour and emulsifying properties of myofibrillar proteins by l-arginine at low and high salt concentration","volume":"56","author":"Guo","year":"2021","journal-title":"Int. J. Food Sci. Technol."},{"key":"10.1016\/j.jcis.2026.139940_bib0018","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.ijbiomac.2017.06.085","article-title":"Thermal aggregation of human immunoglobulin G in arginine solutions: contrasting effects of stabilizers and destabilizers","volume":"104","author":"Yoshizawa","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"issue":"4","key":"10.1016\/j.jcis.2026.139940_bib0019","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1093\/abt\/tbad022","article-title":"Effects of arginine in therapeutic protein formulations: a decade review and perspectives","volume":"6","author":"Ren","year":"2023","journal-title":"Antibody Ther."},{"issue":"4","key":"10.1016\/j.jcis.2026.139940_bib0020","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1016\/j.xphs.2021.11.018","article-title":"Arginine and its derivatives suppress the opalescence of an antibody solution","volume":"111","author":"Oki","year":"2022","journal-title":"J. Pharm. Sci."},{"issue":"43","key":"10.1016\/j.jcis.2026.139940_bib0021","doi-asserted-by":"crossref","first-page":"11225","DOI":"10.1021\/acs.iecr.6b02042","article-title":"Viscosity reduction of a concentrated monoclonal antibody with argininehcl and arginineglutamate","volume":"55","author":"Borwankar","year":"2016","journal-title":"Ind. Eng. Chem. Res."},{"issue":"1","key":"10.1016\/j.jcis.2026.139940_bib0022","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.xphs.2019.06.005","article-title":"Characterization of excipient effects on reversible self-association, backbone flexibility, and solution properties of an IgG1 monoclonal antibody at high concentrations: part 1","volume":"109","author":"Hu","year":"2020","journal-title":"J. Pharm. Sci."},{"issue":"5","key":"10.1016\/j.jcis.2026.139940_bib0023","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1021\/bp0498793","article-title":"Role of arginine in protein refolding, solubilization, and purification","volume":"20","author":"Tsumoto","year":"2004","journal-title":"Biotechnol. Prog."},{"issue":"12","key":"10.1016\/j.jcis.2026.139940_bib0024","doi-asserted-by":"crossref","first-page":"4478","DOI":"10.1021\/acs.molpharmaceut.5b00643","article-title":"Viscosity-lowering effect of amino acids and salts on highly concentrated solutions of two IgG1 monoclonal antibodies","volume":"12","author":"Wang","year":"2015","journal-title":"Mol. Pharm."},{"issue":"8","key":"10.1016\/j.jcis.2026.139940_bib0025","doi-asserted-by":"crossref","first-page":"2517","DOI":"10.1016\/j.xphs.2019.03.008","article-title":"Enhancing stability and reducing viscosity of a monoclonal antibody with cosolutes by weakening protein-protein interactions","volume":"108","author":"Dear","year":"2019","journal-title":"J. Pharm. Sci."},{"issue":"11","key":"10.1016\/j.jcis.2026.139940_bib0026","doi-asserted-by":"crossref","first-page":"5563","DOI":"10.1021\/acs.molpharmaceut.3c00484","article-title":"Characterizing protein-protein interactions and viscosity of a monoclonal antibody from low to high concentration using small-angle x-ray scattering and molecular dynamics simulations","volume":"20","author":"Chowdhury","year":"2023","journal-title":"Mol. Pharm."},{"issue":"6","key":"10.1016\/j.jcis.2026.139940_bib0027","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1021\/mp5000218","article-title":"Specific decrease in solution viscosity of antibodies by arginine for therapeutic formulations","volume":"11","author":"Inoue","year":"2014","journal-title":"Mol. Pharm."},{"issue":"1\u20132","key":"10.1016\/j.jcis.2026.139940_bib0028","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ijpharm.2016.09.003","article-title":"Arginine as a protein stabilizer and destabilizer in liquid formulations","volume":"513","author":"Kim","year":"2016","journal-title":"Int. J. Pharm."},{"issue":"1","key":"10.1016\/j.jcis.2026.139940_bib0029","doi-asserted-by":"crossref","first-page":"3984","DOI":"10.1038\/s41598-017-04409-x","article-title":"A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives","volume":"7","author":"Borzova","year":"2017","journal-title":"Sci. Rep."},{"issue":"29","key":"10.1016\/j.jcis.2026.139940_bib0030","doi-asserted-by":"crossref","first-page":"19146","DOI":"10.1021\/acs.langmuir.5c01237","article-title":"Air-water interfacial adsorption of the chaperone protein DNAJB6b","volume":"41","author":"Pallbo","year":"2025","journal-title":"Langmuir"},{"key":"10.1016\/j.jcis.2026.139940_bib0031","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.jcis.2024.06.111","article-title":"Interfacial mechanics of \u03b2-casein and albumin mixed protein assemblies at liquid-liquid interfaces","volume":"674","author":"Chrysanthou","year":"2024","journal-title":"J. Colloid Interface Sci."},{"issue":"27","key":"10.1016\/j.jcis.2026.139940_bib0032","doi-asserted-by":"crossref","first-page":"7814","DOI":"10.1021\/acs.langmuir.0c00797","article-title":"Competitive surface activity of monoclonal antibodies and nonionic surfactants at the air-water interface determined by interfacial rheology and neutron reflectometry","volume":"36","author":"Tein","year":"2020","journal-title":"Langmuir"},{"key":"10.1016\/j.jcis.2026.139940_bib0033","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.jcis.2019.04.060","article-title":"Linking aggregation and interfacial properties in monoclonal antibody-surfactant formulations","volume":"550","author":"Kannan","year":"2019","journal-title":"J. Colloid Interface Sci."},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0034","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/BF02707140","article-title":"Interfacial tension kinetics of nisin and \u03b2 -casein at an oil-water interface","volume":"17","author":"Lee","year":"2000","journal-title":"Korean J. Chem. Eng."},{"issue":"50","key":"10.1016\/j.jcis.2026.139940_bib0035","first-page":"13228","article-title":"Probing shear thinning behaviors of IgG molecules at the air-water interface","volume":"32","author":"Gleason","year":"2016","journal-title":"Langmuir"},{"issue":"1\u20133","key":"10.1016\/j.jcis.2026.139940_bib0036","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.colsurfa.2006.11.054","article-title":"Behaviour of BSA and of BSA-derivatives at the air\/water interface","volume":"301","author":"Berthold","year":"2007","journal-title":"Colloids Surf., A"},{"key":"10.1016\/j.jcis.2026.139940_bib0037","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/s00397-009-0407-3","article-title":"A double wall-ring geometry for interfacial shear rheometry","volume":"49","author":"Vandebril","year":"2010","journal-title":"Rheol Acta"},{"issue":"6","key":"10.1016\/j.jcis.2026.139940_bib0038","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1122\/1.2970095","article-title":"New measures for characterizing nonlinear viscoelasticity in large amplitude oscillatory shear","volume":"52","author":"Ewoldt","year":"2008","journal-title":"J. Rheol."},{"issue":"5","key":"10.1016\/j.jcis.2026.139940_bib0039","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1122\/1.5127743","article-title":"Characterization and rheology of platelet-rich plasma","volume":"64","author":"Mitra","year":"2020","journal-title":"J. Rheol."},{"key":"10.1016\/j.jcis.2026.139940_bib0040","series-title":"Rheological and lipid characterization of minipig and human skin tissue: a comparative study across different locations and depths","first-page":"1","author":"Mitra","year":"2024"},{"key":"10.1016\/j.jcis.2026.139940_bib0041","volume":"140","author":"Hou","year":"2021","journal-title":"Mech. Dominat. Thixotropy Limestone Calcined Clay Cement (LC3)"},{"key":"10.1016\/j.jcis.2026.139940_bib0042","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.foodhyd.2013.07.017","article-title":"Dynamic rheological properties of lepidium perfoliatum seed gum: effect of concentration, temperature and heating\/cooling rate","volume":"35","author":"Hesarinejad","year":"2014","journal-title":"Food Hydrocoll."},{"issue":"11","key":"10.1016\/j.jcis.2026.139940_bib0043","doi-asserted-by":"crossref","first-page":"5150","DOI":"10.1039\/c0sm01312a","article-title":"Rheology of globular proteins: apparent yield stress, high shear rate viscosity and interfacial viscoelasticity of bovine serum albumin solutions","volume":"7","author":"Sharma","year":"2011","journal-title":"Soft Matter"},{"key":"10.1016\/j.jcis.2026.139940_bib0044","doi-asserted-by":"crossref","first-page":"7623","DOI":"10.1039\/c1sm05399j","article-title":"Interfacial viscoelasticity, yielding and creep ringing of globular protein-surfactant mixtures","volume":"7","author":"Jaishankar","year":"2011","journal-title":"Soft Matter"},{"issue":"1","key":"10.1016\/j.jcis.2026.139940_bib0045","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1006\/jcis.1997.4803","article-title":"Interfacial rheological and tension properties of protein films","volume":"189","author":"Burgess","year":"1997","journal-title":"J. Colloid Interface Sci."},{"issue":"9","key":"10.1016\/j.jcis.2026.139940_bib0046","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1002\/polb.23463","article-title":"Experimental clues of soft glassy rheology in strained filled elastomers","volume":"52","author":"Ehrburger-Dolle","year":"2014","journal-title":"J. Polym. Sci., Part B"},{"issue":"4","key":"10.1016\/j.jcis.2026.139940_bib0047","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1122\/8.0000808","article-title":"Nonlinear oscillatory rheology of aqueous suspensions of cellulose nanocrystals and nanofibrils","volume":"68","author":"Xu","year":"2024","journal-title":"J. Rheol."},{"key":"10.1016\/j.jcis.2026.139940_bib0048","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2020.106172","article-title":"Van der goot, small and large oscillatory shear properties of concentrated proteins","volume":"110","author":"Schreuders","year":"2021","journal-title":"Food Hydrocoll."},{"issue":"12","key":"10.1016\/j.jcis.2026.139940_bib0049","doi-asserted-by":"crossref","first-page":"4830","DOI":"10.1002\/jps.22198","article-title":"Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies","volume":"99","author":"Sahin","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.jcis.2026.139940_bib0050","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.jchromb.2017.09.033","article-title":"Determination of isoelectric points and relative charge variants of 23 therapeutic monoclonal antibodies","volume":"1065","author":"Goyon","year":"2017","journal-title":"J. Chromatogr. B"},{"issue":"12","key":"10.1016\/j.jcis.2026.139940_bib0051","doi-asserted-by":"crossref","first-page":"3835","DOI":"10.1021\/jp037236k","article-title":"Interfacial rheology of globular and flexible proteins at the hexadecane\/water interface: comparison of shear and dilatation deformation","volume":"108","author":"Freer","year":"2004","journal-title":"J. Phys. Chem. B"},{"issue":"23","key":"10.1016\/j.jcis.2026.139940_bib0052","doi-asserted-by":"crossref","first-page":"10159","DOI":"10.1021\/la0485226","article-title":"Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane\/water interface","volume":"20","author":"Freer","year":"2004","journal-title":"Langmuir"},{"issue":"1","key":"10.1016\/j.jcis.2026.139940_bib0053","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0301-4622(99)00082-4","article-title":"Protein adsorption at the oil\/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements","volume":"81","author":"Beverung","year":"1999","journal-title":"Biophys. Chem."},{"issue":"3","key":"10.1016\/j.jcis.2026.139940_bib0054","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S0001-8686(00)00077-4","article-title":"Interfacial rheological properties of adsorbed protein layers and surfactants: a review","volume":"91","author":"Bos","year":"2001","journal-title":"Adv. Colloid Interface Sci."},{"issue":"2","key":"10.1016\/j.jcis.2026.139940_bib0055","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0927-7765(99)00042-9","article-title":"Adsorbed protein layers at fluid interfaces: interactions, structure and surface rheology","volume":"15","author":"Dickinson","year":"1999","journal-title":"Colloids Surf., B"},{"issue":"3","key":"10.1016\/j.jcis.2026.139940_bib0056","doi-asserted-by":"crossref","first-page":"19","DOI":"10.3390\/antib5030019","article-title":"Antibody aggregation: insights from sequence and structure","volume":"5","author":"Li","year":"2016","journal-title":"Antibodies"},{"issue":"21","key":"10.1016\/j.jcis.2026.139940_bib0057","doi-asserted-by":"crossref","first-page":"8331","DOI":"10.1073\/pnas.87.21.8331","article-title":"A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor","volume":"87","author":"Kohno","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"148","key":"10.1016\/j.jcis.2026.139940_bib0058","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.2000954","article-title":"Solution of the structure of the tnf-tnfr2 complex","volume":"3","author":"Mukai","year":"2010","journal-title":"Sci. Signal."},{"issue":"6","key":"10.1016\/j.jcis.2026.139940_bib0059","doi-asserted-by":"crossref","first-page":"761","DOI":"10.4161\/mabs.22276","article-title":"Characterization and comparison of commercially available tnf receptor 2-fc fusion protein products","volume":"4","author":"Tan","year":"2012","journal-title":"mAbs"},{"key":"10.1016\/j.jcis.2026.139940_bib0060","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.jcis.2023.12.068","article-title":"Role of the pea protein aggregation state on their interfacial properties","volume":"658","author":"Grasberger","year":"2024","journal-title":"J. Colloid Interface Sci."},{"issue":"7","key":"10.1016\/j.jcis.2026.139940_bib0061","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1002\/pro.3382","article-title":"Protein-protein interactions controlling interfacial aggregation of rhil-1ra are not described by simple colloid models","volume":"27","author":"Sorret","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.jcis.2026.139940_bib0062","series-title":"Surface Dilational Rheology of Proteins Adsorbed at Air\/Water and Oil\/Water Interfaces","volume":"7","author":"Benjamins","year":"1998"},{"issue":"45","key":"10.1016\/j.jcis.2026.139940_bib0063","doi-asserted-by":"crossref","first-page":"9724","DOI":"10.1021\/acs.jpcb.3c05900","article-title":"Interfacial pressure and viscoelasticity of antibodies and their correlation to long-term stability in formulation","volume":"127","author":"Pham","year":"2023","journal-title":"J. Phys. Chem. B"},{"issue":"35","key":"10.1016\/j.jcis.2026.139940_bib0064","doi-asserted-by":"crossref","first-page":"12779","DOI":"10.1021\/la302258k","article-title":"How do proteins unfold upon adsorption on nanoparticle surfaces?","volume":"28","author":"Pan","year":"2012","journal-title":"Langmuir"},{"issue":"35","key":"10.1016\/j.jcis.2026.139940_bib0065","doi-asserted-by":"crossref","first-page":"16946","DOI":"10.1021\/jp050990g","article-title":"Quantitative description of the relation between protein net charge and protein adsorption to air-water interfaces","volume":"109","author":"Wierenga","year":"2005","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jcis.2026.139940_bib0066","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.jcis.2018.11.054","article-title":"Determining the surface dilational rheology of surfactant and protein films with a droplet waveform generator","volume":"537","author":"Yang","year":"2019","journal-title":"J. Colloid Interface Sci."},{"issue":"4","key":"10.1016\/j.jcis.2026.139940_bib0067","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1002\/jps.24358","article-title":"Gelation of a monoclonal antibody at the silicone oil-water interface and subsequent rupture of the interfacial gel results in aggregation and particle formation","volume":"104","author":"Mehta","year":"2015","journal-title":"J. Pharm. Sci."},{"issue":"10","key":"10.1016\/j.jcis.2026.139940_bib0068","doi-asserted-by":"crossref","first-page":"4745","DOI":"10.1021\/acs.molpharmaceut.8b00706","article-title":"Viscosities and protein interactions of bispecific antibodies and their monospecific mixtures","volume":"15","author":"Woldeyes","year":"2018","journal-title":"Mol. Pharm."},{"issue":"12","key":"10.1016\/j.jcis.2026.139940_bib0069","doi-asserted-by":"crossref","first-page":"4812","DOI":"10.1002\/jps.22190","article-title":"Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies","volume":"99","author":"Yadav","year":"2010","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.jcis.2026.139940_bib0070","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.ejpb.2020.06.007","article-title":"Micro- and macro-viscosity relations in high concentration antibody solutions","volume":"153","author":"Shah","year":"2020","journal-title":"Eur. J. Pharm. Biopharm."}],"container-title":["Journal of Colloid and Interface Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021979726001177?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021979726001177?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T13:03:31Z","timestamp":1779282211000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021979726001177"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5]]},"references-count":70,"alternative-id":["S0021979726001177"],"URL":"https:\/\/doi.org\/10.1016\/j.jcis.2026.139940","relation":{},"ISSN":["0021-9797"],"issn-type":[{"value":"0021-9797","type":"print"}],"subject":[],"published":{"date-parts":[[2026,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effects of arginine on the interfacial behavior of proteins","name":"articletitle","label":"Article Title"},{"value":"Journal of Colloid and Interface Science","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jcis.2026.139940","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"139940"}}