{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,18]],"date-time":"2025-11-18T12:26:15Z","timestamp":1763468775614,"version":"build-2065373602"},"reference-count":70,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2022,6,25]],"date-time":"2022-06-25T00:00:00Z","timestamp":1656115200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Polymers"],"abstract":"<jats:p>Nowadays, tuberculosis is the second leading cause of death from a monopathogenic transmitted disease, only ahead of COVID-19. The role of exported repetitive protein (Erp) in the virulence of Mycobacterium tuberculosis has been extensively demonstrated. In vitro and in vivo assays have identified that Erp interacts with Rv1417 and Rv2617c proteins, forming putative transient molecular complexes prior to localization to the cell envelope. Although new insights into the interactions and functions of Erp have emerged over the years, knowledge about its structure and protein\u2013protein interactions at the atomistic level has not been sufficiently explored. In this work, we have combined several in silico methodologies to gain new insights into the structural relationship between these proteins. Two system conditions were evaluated by MD simulations: Rv1417 and Rv2617c embedded in a lipid membrane and another with a semi-polar solvent to mimic the electrostatic conditions on the membrane surface. The Erp protein was simulated as an unanchored structure. Stabilized structures were docked, and complexes were evaluated to recognize the main residues involved in protein\u2013protein interactions. Our results show the influence of the medium on the structural conformation of proteins. Globular conformations were favored under high polarity conditions and showed a higher energetic affinity in complex formation. Meanwhile, disordered conformations were favored under semi-polar conditions and an increase in the number of contacts between residues was observed. In addition, the electrostatic potential analysis showed remarkable changes in protein interactions due to the polarity of the medium, demonstrating the relevance of Erp protein in heterodimer formation. On the other hand, contact analysis showed that several C-terminal residues of Erp were involved in the protein interactions, which seems to contradict experimental observations; however, these complexes could be transient forms. The findings presented in this work are intended to open new perspectives in the studies of Erp protein molecular interactions and to improve the knowledge about its function and role in the virulence of Mycobacterium tuberculosis.<\/jats:p>","DOI":"10.3390\/polym14132577","type":"journal-article","created":{"date-parts":[[2022,6,26]],"date-time":"2022-06-26T21:01:41Z","timestamp":1656277301000},"page":"2577","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Novel In Silico Insights into Rv1417 and Rv2617c as Potential Protein Targets: The Importance of the Medium on the Structural Interactions with Exported Repetitive Protein (Erp) of Mycobacterium tuberculosis"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2674-4281","authenticated-orcid":false,"given":"Margot","family":"Paco-Chipana","sequence":"first","affiliation":[{"name":"Centro de Investigaci\u00f3n en Ingenier\u00eda Molecular\u2014CIIM, Universidad Cat\u00f3lica de Santa Mar\u00eda, Urb. San Jos\u00e9 s\/n\u2014Umacollo, Arequipa 04000, Peru"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9305-7003","authenticated-orcid":false,"given":"Camilo","family":"Febres-Molina","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n en Ingenier\u00eda Molecular\u2014CIIM, Universidad Cat\u00f3lica de Santa Mar\u00eda, Urb. San Jos\u00e9 s\/n\u2014Umacollo, Arequipa 04000, Peru"},{"name":"Doctorado en Fisicoqu\u00edmica Molecular, Facultad de Ciencias Exactas, Universidad Andr\u00e9s Bello, Santiago 8320000, Chile"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2921-5681","authenticated-orcid":false,"given":"Jorge Alberto","family":"Aguilar-Pineda","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n en Ingenier\u00eda Molecular\u2014CIIM, Universidad Cat\u00f3lica de Santa Mar\u00eda, Urb. 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J."},{"key":"ref_2","first-page":"288","article-title":"Diabetes y tuberculosis: Una sindemia complicada por la COVID-19","volume":"157","year":"2021","journal-title":"Med. Cl\u00edn."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e1132","DOI":"10.1016\/S2214-109X(20)30288-6","article-title":"Potential impact of the COVID-19 pandemic on HIV, tuberculosis, and malaria in low-income and middle-income countries: A modelling study","volume":"8","author":"Hogan","year":"2020","journal-title":"Lancet Glob. Health"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1056\/NEJMp2118145","article-title":"COVID-19\u2019s Devastating Effect on Tuberculosis Care\u2014A Path to Recovery","volume":"386","author":"Pai","year":"2022","journal-title":"N. Engl. J. Med."},{"unstructured":"WHO (2021). Global Tuberculosis Report 2021, World Health Organization.","key":"ref_5"},{"unstructured":"(2022, March 25). Tuberculosis. Available online: https:\/\/www.who.int\/es\/news-room\/fact-sheets\/detail\/tuberculosis.","key":"ref_6"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"143","DOI":"10.4103\/0974-777X.81691","article-title":"Tuberculosis: Current situation, challenges and overview of its control programs in India","volume":"3","author":"Sandhu","year":"2011","journal-title":"J. Glob. Infect. Dis."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.chom.2020.11.013","article-title":"The immune landscape in tuberculosis reveals populations linked to disease and latency","volume":"29","author":"Esaulova","year":"2021","journal-title":"Cell Host Microbe"},{"doi-asserted-by":"crossref","unstructured":"Mori, G., Morrison, M., and Blumenthal, A. (2021). Microbiome-immune interactions in tuberculosis. PLoS Pathog., 17.","key":"ref_9","DOI":"10.1371\/journal.ppat.1009377"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"367","DOI":"10.11113\/mjfas.v15n3.1030","article-title":"Synthesis and molecular docking of isonicotinohydrazide derivatives as anti-tuberculosis candidates","volume":"15","author":"Ruswanto","year":"2019","journal-title":"Malays. J. Fundam. Appl. Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1080\/07391102.2017.1341337","article-title":"Structure-based screening and molecular dynamics simulations offer novel natural compounds as potential inhibitors of Mycobacterium tuberculosis isocitrate lyase","volume":"36","author":"Shukla","year":"2018","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.coph.2021.05.007","article-title":"Novel treatments in multidrug-resistant tuberculosis","volume":"59","author":"Mondoni","year":"2021","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.1080\/07391102.2017.1384398","article-title":"Discovery of novel inhibitors of Mycobacterium tuberculosis MurG: Homology modelling, structure based pharmacophore, molecular docking, and molecular dynamics simulations","volume":"36","author":"Saxena","year":"2018","journal-title":"J. Biomol. Struct. Dyn."},{"doi-asserted-by":"crossref","unstructured":"Kumar, M., Singh, S.K., Singh, P.P., Singh, V.K., Rai, A.C., Srivastava, A.K., Shukla, L., Kesawat, M.S., Kumar Jaiswal, A., and Chung, S.M. (2021). Potential Anti-Mycobacterium tuberculosis Activity of Plant Secondary Metabolites: Insight with Molecular Docking Interactions. Antioxidants, 10.","key":"ref_14","DOI":"10.3390\/antiox10121990"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1128\/JB.00120-16","article-title":"Interaction of Erp protein of Mycobacterium tuberculosis with Rv2212 enhances intracellular survival of Mycobacterium smegmatis","volume":"198","author":"Ganaie","year":"2016","journal-title":"J. Bacteriol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"65","DOI":"10.3389\/fcimb.2020.00065","article-title":"Mycobacterium tuberculosis dissemination plays a critical role in pathogenesis","volume":"10","author":"Moule","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.mib.2020.01.011","article-title":"Mycobacterium tuberculosis pathogenicity viewed through the lens of molecular Koch\u2019s postulates","volume":"54","author":"Ramakrishnan","year":"2020","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"eaba6944","DOI":"10.1126\/sciadv.aba6944","article-title":"VapBC22 toxin-antitoxin system from Mycobacterium tuberculosis is required for pathogenesis and modulation of host immune response","volume":"6","author":"Agarwal","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.meegid.2018.12.013","article-title":"Update on the virulence factors of the obligate pathogen Mycobacterium tuberculosis and related tuberculosis-causing mycobacteria","volume":"72","author":"Madacki","year":"2019","journal-title":"Infect. Genet. Evol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1128\/IAI.72.4.2379-2382.2004","article-title":"The hydrophobic domain of the mycobacterial Erp protein is not essential for the virulence of Mycobacterium tuberculosis","volume":"72","author":"Bordat","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1128\/IAI.02061-05","article-title":"Mycobacterium marinum Erp is a virulence determinant required for cell wall integrity and intracellular survival","volume":"74","author":"Cosma","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1126\/science.282.5389.759","article-title":"Attenuation of virulence by disruption of the Mycobacterium tuberculosis erp gene","volume":"282","author":"Berthet","year":"1998","journal-title":"Science"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1080\/21505594.2019.1693714","article-title":"Rv2617c and P36 are virulence factors of pathogenic mycobacteria involved in resistance to oxidative stress","volume":"10","author":"Forrellad","year":"2019","journal-title":"Virulence"},{"doi-asserted-by":"crossref","unstructured":"Klepp, L.I., Soria, M., Blanco, F.C., Bianco, M.V., Santangelo, M.P., Cataldi, A.A., and Bigi, F. (2009). Identification of two proteins that interact with the Erp virulence factor from Mycobacterium tuberculosis by using the bacterial two-hybrid system. BMC Mol. Biol., 10.","key":"ref_24","DOI":"10.1186\/1471-2199-10-3"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2123","DOI":"10.1099\/13500872-141-9-2123","article-title":"Characterization of the Mycobacterium tuberculosis erp gene encoding a potential cell surface protein with repetitive structures","volume":"141","author":"Berthet","year":"1995","journal-title":"Microbiology"},{"unstructured":"(2021, September 20). Exported Repetitive Protein, Accession Code P9WIQ7. Available online: https:\/\/www.uniprot.org\/uniprot\/P9WIQ7.","key":"ref_26"},{"unstructured":"(2021, September 20). Uncharacterized Protein Rv1417, Accession Code P9WLY1. Available online: https:\/\/www.uniprot.org\/uniprot\/P9WLY1.","key":"ref_27"},{"unstructured":"(2021, September 20). Probable Transmembrane Protein, Accession Code I6XER9. Available online: https:\/\/www.uniprot.org\/uniprot\/I6XER9.","key":"ref_28"},{"unstructured":"Uniprot (2021). UniProt: The universal protein knowledgebase in 2021. Nucleic Acids Res., 49, D480\u2013D489.","key":"ref_29"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"D439","DOI":"10.1093\/nar\/gkab1061","article-title":"AlphaFold Protein Structure Database: Massively expanding the structural coverage of protein-sequence space with high-accuracy models","volume":"50","author":"Varadi","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/nprot.2010.5","article-title":"I-TASSER: A unified platform for automated protein structure and function prediction","volume":"5","author":"Roy","year":"2010","journal-title":"Nat. Protoc."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nmeth.3213","article-title":"The I-TASSER Suite: Protein structure and function prediction","volume":"12","author":"Yang","year":"2015","journal-title":"Nat. Methods"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"W174","DOI":"10.1093\/nar\/gkv342","article-title":"I-TASSER server: New development for protein structure and function predictions","volume":"43","author":"Yang","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2525","DOI":"10.1016\/j.bpj.2011.10.024","article-title":"Improving the physical realism and structural accuracy of protein models by a two-step atomic-level energy minimization","volume":"101","author":"Xu","year":"2011","journal-title":"Biophys. J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/j.ymeth.2006.08.006","article-title":"Setting up and running molecular dynamics simulations of membrane proteins","volume":"41","author":"Kandt","year":"2007","journal-title":"Methods"},{"unstructured":"Lide, D.R. (2010). CRC Handbook of Chemistry and Physics, CRC Press.","key":"ref_37"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1002\/jcc.26011","article-title":"More bang for your buck: Improved use of GPU nodes for GROMACS 2018","volume":"40","author":"Kutzner","year":"2019","journal-title":"J. Comput. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"11225","DOI":"10.1021\/ja9621760","article-title":"Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids","volume":"118","author":"Jorgensen","year":"1996","journal-title":"J. Am. Chem. Soc."},{"doi-asserted-by":"crossref","unstructured":"Duhovny, D., Nussinov, R., and Wolfson, H.J. (2002, January 17\u201321). Efficient unbound docking of rigid molecules. Proceedings of the International Workshop on Algorithms in Bioinformatics, Rome, Italy.","key":"ref_42","DOI":"10.1007\/3-540-45784-4_14"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"W363","DOI":"10.1093\/nar\/gki481","article-title":"PatchDock and SymmDock: Servers for rigid and symmetric docking","volume":"33","author":"Inbar","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1002\/prot.21495","article-title":"FireDock: Fast interaction refinement in molecular docking","volume":"69","author":"Andrusier","year":"2007","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"W229","DOI":"10.1093\/nar\/gkn186","article-title":"FireDock: A web server for fast interaction refinement in molecular docking","volume":"36","author":"Mashiach","year":"2008","journal-title":"Nucleic Acids Res."},{"doi-asserted-by":"crossref","unstructured":"Hurwitz, N., and Wolfson, H.J. (2021). Memdock: An \u03b1-Helical Membrane Protein Docking Algorithm. Computational Design of Membrane Proteins, Springer.","key":"ref_46","DOI":"10.1007\/978-1-0716-1468-6_7"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: Visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"doi-asserted-by":"crossref","unstructured":"Turner, P.J. (2005). XMGRACE, Version 5.1.19.","key":"ref_49","DOI":"10.7748\/ns.19.22.22.s31"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/protein\/8.2.127","article-title":"LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions","volume":"8","author":"Wallace","year":"1995","journal-title":"Protein Eng. Des. Sel."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: Application to microtubules and the ribosome","volume":"98","author":"Baker","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"W665","DOI":"10.1093\/nar\/gkh381","article-title":"PDB2PQR: An automated pipeline for the setup of Poisson\u2013Boltzmann electrostatics calculations","volume":"32","author":"Dolinsky","year":"2004","journal-title":"Nucleic Acids Res."},{"unstructured":"(2019). Mathematica, Wolfram Research, Inc.. Version 12.0.","key":"ref_53"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.bbrc.2014.05.111","article-title":"Membrane topology of transmembrane proteins: Determinants and experimental tools","volume":"453","author":"Lee","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"551","DOI":"10.2174\/1389450120666181204164721","article-title":"Understanding membrane protein drug targets in computational perspective","volume":"20","author":"Gong","year":"2019","journal-title":"Curr. Drug Targets"},{"doi-asserted-by":"crossref","unstructured":"Hallgren, J., Tsirigos, K.D., Pedersen, M.D., Armenteros, J.J.A., Marcatili, P., Nielsen, H., Krogh, A., and Winther, O. (2022). DeepTMHMM predicts alpha and beta transmembrane proteins using deep neural networks. bioRxiv.","key":"ref_56","DOI":"10.1101\/2022.04.08.487609"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1002\/prot.21798","article-title":"Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature","volume":"71","author":"Kumar","year":"2008","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1039\/b905518p","article-title":"Unraveling the potential of intrinsically disordered proteins as drug targets: Application to Mycobacterium tuberculosis","volume":"5","author":"Anurag","year":"2009","journal-title":"Mol. BioSyst."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1038\/nrm3920","article-title":"Intrinsically disordered proteins in cellular signalling and regulation","volume":"16","author":"Wright","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1080\/07391102.2018.1454852","article-title":"Drug targeted virtual screening and molecular dynamics of LipU protein of Mycobacterium tuberculosis and Mycobacterium leprae","volume":"37","author":"Kaur","year":"2019","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"W329","DOI":"10.1093\/nar\/gky384","article-title":"IUPred2A: Context-dependent prediction of protein disorder as a function of redox state and protein binding","volume":"46","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"e99","DOI":"10.1002\/cpbi.99","article-title":"Analyzing protein disorder with IUPred2A","volume":"70","year":"2020","journal-title":"Curr. Protoc. Bioinform."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S0006-3495(03)74565-2","article-title":"Low dielectric permittivity of water at the membrane interface: Effect on the energy coupling mechanism in biological membranes","volume":"85","author":"Cherepanov","year":"2003","journal-title":"Biophys. J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.bpj.2017.12.013","article-title":"Structural impact of phosphorylation and dielectric constant variation on synaptotagmin\u2019s IDR","volume":"114","author":"Fealey","year":"2018","journal-title":"Biophys. J."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"8246","DOI":"10.1021\/bi990510+","article-title":"Water-soluble \u03b2-sheet models which self-assemble into fibrillar structures","volume":"38","author":"Janek","year":"1999","journal-title":"Biochemistry"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"118","DOI":"10.3109\/09687688.2012.678018","article-title":"Resolving the kinetics of lipid, protein and peptide diffusion in membranes","volume":"29","author":"Sanderson","year":"2012","journal-title":"Mol. Membr. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"3951","DOI":"10.1529\/biophysj.105.076596","article-title":"Molecular simulation study of structural and dynamic properties of mixed DPPC\/DPPE bilayers","volume":"90","author":"Leekumjorn","year":"2006","journal-title":"Biophys. J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"13805","DOI":"10.1021\/acs.langmuir.9b02538","article-title":"Lipid bilayer thickness measured by quantitative DIC reveals phase transitions and effects of substrate hydrophilicity","volume":"35","author":"Regan","year":"2019","journal-title":"Langmuir"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/pro.3280","article-title":"Improvements to the APBS biomolecular solvation software suite","volume":"27","author":"Jurrus","year":"2018","journal-title":"Protein Sci."}],"container-title":["Polymers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4360\/14\/13\/2577\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:40:02Z","timestamp":1760139602000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4360\/14\/13\/2577"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,6,25]]},"references-count":70,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2022,7]]}},"alternative-id":["polym14132577"],"URL":"https:\/\/doi.org\/10.3390\/polym14132577","relation":{},"ISSN":["2073-4360"],"issn-type":[{"type":"electronic","value":"2073-4360"}],"subject":[],"published":{"date-parts":[[2022,6,25]]}}}