{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T10:16:15Z","timestamp":1788516975340,"version":"build-2803163510"},"reference-count":102,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:00:00Z","timestamp":1788480000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:00:00Z","timestamp":1788480000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-026-60957-1","type":"journal-article","created":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T09:50:45Z","timestamp":1788515445000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Antimicrobial peptides as computational candidates for SARS-CoV-2 papain-like protease inhibition"],"prefix":"10.1038","volume":"16","author":[{"given":"Erenilson","family":"dos Santos Moreira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergio","family":"Siqueira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabricio Santos","family":"Barbosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jailan","family":"da Silva Sousa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hugo Mauricio Pe\u00f1a","family":"Mercado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tarcisio Silva","family":"Melo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arun Kumar","family":"Jaiswal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vasco","family":"Azevedo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arist\u00f3teles","family":"G\u00f3es-Neto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8031-9454","authenticated-orcid":false,"given":"Bruno Silva","family":"Andrade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,9,4]]},"reference":[{"key":"60957_CR1","doi-asserted-by":"publisher","first-page":"109721","DOI":"10.1016\/j.cellsig.2020.109721","volume":"74","author":"R Poduri","year":"2020","unstructured":"Poduri, R., Joshi, G. & Jagadeesh, G. Drugs targeting various stages of the SARS-CoV-2 life cycle: Exploring promising drugs for the treatment of Covid-19. Cell. Signal. 74, 109721. https:\/\/doi.org\/10.1016\/j.cellsig.2020.109721 (2020).","journal-title":"Cell. Signal."},{"key":"60957_CR2","doi-asserted-by":"publisher","first-page":"e00855","DOI":"10.1128\/jvi.00855-24","volume":"98","author":"AF Rhamadianti","year":"2024","unstructured":"Rhamadianti, A. F. et al. SARS-CoV-2 papain-like protease inhibits ISGylation of the viral nucleocapsid protein to evade host anti-viral immunity. J. Virol. 98, e00855\u2013e00824. https:\/\/doi.org\/10.1128\/jvi.00855-24 (2024).","journal-title":"J. Virol."},{"key":"60957_CR3","doi-asserted-by":"publisher","first-page":"EMBJ2020106275","DOI":"10.15252\/embj.2020106275","volume":"39","author":"T Klemm","year":"2020","unstructured":"Klemm, T. et al. Mechanism and inhibition of the papain-like protease, PLpro, of SARS\u2010CoV\u20102. EMBO J. 39, EMBJ2020106275. https:\/\/doi.org\/10.15252\/embj.2020106275 (2020).","journal-title":"EMBO J."},{"key":"60957_CR4","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1038\/s41467-021-21060-3","volume":"12","author":"J Osipiuk","year":"2021","unstructured":"Osipiuk, J. et al. Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors. Nat. Commun. 12, 743. https:\/\/doi.org\/10.1038\/s41467-021-21060-3 (2021).","journal-title":"Nat. Commun."},{"key":"60957_CR5","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1038\/s41579-020-00468-6","volume":"19","author":"P V\u2019kovski","year":"2021","unstructured":"V\u2019kovski, P. et al. Coronavirus biology and replication: implications for SARS-CoV-2. Nat. Rev. Microbiol. 19, 155\u2013170. https:\/\/doi.org\/10.1038\/s41579-020-00468-6 (2021).","journal-title":"Nat. Rev. Microbiol."},{"key":"60957_CR6","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1038\/s41573-023-00672-y","volume":"22","author":"G Li","year":"2023","unstructured":"Li, G., Hilgenfeld, R., Whitley, R. & De Clercq, E. Therapeutic strategies for COVID-19: progress and lessons learned. Nat. Rev. Drug Discov. 22, 449\u2013475. https:\/\/doi.org\/10.1038\/s41573-023-00672-y (2023).","journal-title":"Nat. Rev. Drug Discov"},{"key":"60957_CR7","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1038\/s41467-020-20718-8","volume":"12","author":"Z Fu","year":"2021","unstructured":"Fu, Z. et al. The complex structure of GRL0617 and SARS-CoV-2 PLpro reveals a hot spot for antiviral drug discovery. Nat. Commun. 12, 488. https:\/\/doi.org\/10.1038\/s41467-020-20718-8 (2021).","journal-title":"Nat. Commun."},{"key":"60957_CR8","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1038\/s41586-020-2601-5","volume":"587","author":"D Shin","year":"2020","unstructured":"Shin, D. et al. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature 587, 657\u2013662. https:\/\/doi.org\/10.1038\/s41586-020-2601-5 (2020).","journal-title":"Nature"},{"key":"60957_CR9","doi-asserted-by":"publisher","first-page":"4681","DOI":"10.1039\/D3SC00166K","volume":"14","author":"Q Shao","year":"2023","unstructured":"Shao, Q. et al. Unraveling the catalytic mechanism of SARS-CoV-2 papain-like protease with allosteric modulation of C270 mutation using multiscale computational approaches. Chem. Sci. 14, 4681\u20134696. https:\/\/doi.org\/10.1039\/D3SC00166K (2023).","journal-title":"Chem. Sci."},{"key":"60957_CR10","doi-asserted-by":"publisher","first-page":"825","DOI":"10.3390\/pathogens13100825","volume":"13","author":"MA Diogo","year":"2024","unstructured":"Diogo, M. A., Cabral, A. G. T. & De Oliveira, R. B. Advances in the Search for SARS-CoV-2 Mpro and PLpro Inhibitors. Pathogens 13, 825. https:\/\/doi.org\/10.3390\/pathogens13100825 (2024).","journal-title":"Pathogens"},{"key":"60957_CR11","doi-asserted-by":"publisher","first-page":"eabd4596","DOI":"10.1126\/sciadv.abd4596","volume":"6","author":"W Rut","year":"2020","unstructured":"Rut, W. et al. Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti\u2013COVID-19 drug design. Sci. Adv. 6, eabd4596. https:\/\/doi.org\/10.1126\/sciadv.abd4596 (2020).","journal-title":"Sci. Adv."},{"key":"60957_CR12","doi-asserted-by":"publisher","first-page":"103832","DOI":"10.1016\/j.drudis.2023.103832","volume":"29","author":"X Li","year":"2024","unstructured":"Li, X. & Song, Y. Targeting SARS-CoV-2 nonstructural protein 3: Function, structure, inhibition, and perspective in drug discovery. Drug Discov Today. 29, 103832. https:\/\/doi.org\/10.1016\/j.drudis.2023.103832 (2024).","journal-title":"Drug Discov Today"},{"key":"60957_CR13","doi-asserted-by":"publisher","first-page":"106012","DOI":"10.1016\/j.ijantimicag.2020.106012","volume":"56","author":"R Yu","year":"2020","unstructured":"Yu, R. et al. Computational screening of antagonists against the SARS-CoV-2 (COVID-19) coronavirus by molecular docking. Int. J. Antimicrob. Agents. 56, 106012. https:\/\/doi.org\/10.1016\/j.ijantimicag.2020.106012 (2020).","journal-title":"Int. J. Antimicrob. Agents"},{"key":"60957_CR14","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.jiph.2022.11.022","volume":"16","author":"T-H Chen","year":"2023","unstructured":"Chen, T-H. et al. The exploration of phytocompounds theoretically combats SARS-CoV-2 pandemic against virus entry, viral replication and immune evasion. J. Infect. Public. Health. 16, 42\u201354. https:\/\/doi.org\/10.1016\/j.jiph.2022.11.022 (2023).","journal-title":"J. Infect. Public. Health"},{"key":"60957_CR15","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1007\/s13205-024-04032-4","volume":"14","author":"G Sharma","year":"2024","unstructured":"Sharma, G. et al. In silico screening and evaluation of antiviral peptides as inhibitors against ORF9b protein of SARS-CoV-2. 3 Biotech. 14, 192. https:\/\/doi.org\/10.1007\/s13205-024-04032-4 (2024).","journal-title":"3 Biotech."},{"key":"60957_CR16","doi-asserted-by":"publisher","first-page":"5143","DOI":"10.1021\/acsnano.0c02857","volume":"14","author":"Y Han","year":"2020","unstructured":"Han, Y. & Kr\u00e1l, P. Computational Design of ACE2-Based Peptide Inhibitors of SARS-CoV-2. ACS Nano. 14, 5143\u20135147. https:\/\/doi.org\/10.1021\/acsnano.0c02857 (2020).","journal-title":"ACS Nano"},{"key":"60957_CR17","doi-asserted-by":"publisher","first-page":"576","DOI":"10.12688\/f1000research.24074.1","volume":"9","author":"D Barh","year":"2020","unstructured":"Barh, D. et al. Potential chimeric peptides to block the SARS-CoV-2 spike receptor-binding domain. F1000Research 9, 576. https:\/\/doi.org\/10.12688\/f1000research.24074.1 (2020).","journal-title":"F1000Research"},{"key":"60957_CR18","doi-asserted-by":"publisher","first-page":"2703","DOI":"10.1007\/s10989-021-10284-y","volume":"27","author":"Y Behzadipour","year":"2021","unstructured":"Behzadipour, Y. et al. Viral 3CLpro as a Target for Antiviral Intervention Using Milk-Derived Bioactive Peptides. Int. J. Pept. Res. Ther. 27, 2703\u20132716. https:\/\/doi.org\/10.1007\/s10989-021-10284-y (2021).","journal-title":"Int. J. Pept. Res. Ther."},{"key":"60957_CR19","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/s44370-024-00006-5","volume":"2","author":"A Qureshi","year":"2025","unstructured":"Qureshi, A. A review on current status of antiviral peptides. Discov Viruses. 2, 3. https:\/\/doi.org\/10.1007\/s44370-024-00006-5 (2025).","journal-title":"Discov Viruses"},{"key":"60957_CR20","doi-asserted-by":"publisher","first-page":"e40121","DOI":"10.1016\/j.heliyon.2024.e40121","volume":"10","author":"M Neghabi Hajigha","year":"2024","unstructured":"Neghabi Hajigha, M. et al. Antiviral and antibacterial peptides: Mechanisms of action. Heliyon 10, e40121. https:\/\/doi.org\/10.1016\/j.heliyon.2024.e40121 (2024).","journal-title":"Heliyon"},{"key":"60957_CR21","doi-asserted-by":"publisher","first-page":"1417","DOI":"10.3390\/antibiotics11101417","volume":"11","author":"J Talapko","year":"2022","unstructured":"Talapko, J. et al. Antimicrobial Peptides\u2014Mechanisms of Action, Antimicrobial Effects and Clinical Applications. Antibiotics 11, 1417. https:\/\/doi.org\/10.3390\/antibiotics11101417 (2022).","journal-title":"Antibiotics"},{"key":"60957_CR22","doi-asserted-by":"publisher","first-page":"171024","DOI":"10.1016\/j.peptides.2023.171024","volume":"166","author":"UL Urmi","year":"2023","unstructured":"Urmi, U. L. et al. A review of the antiviral activity of cationic antimicrobial peptides. Peptides 166, 171024. https:\/\/doi.org\/10.1016\/j.peptides.2023.171024 (2023).","journal-title":"Peptides"},{"key":"60957_CR23","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1016\/j.colsurfb.2016.02.003","volume":"141","author":"A Hollmann","year":"2016","unstructured":"Hollmann, A. et al. Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide\u2013membrane interactions of three related antimicrobial peptides. Colloids Surf. B Biointerfaces. 141, 528\u2013536. https:\/\/doi.org\/10.1016\/j.colsurfb.2016.02.003 (2016).","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"60957_CR24","doi-asserted-by":"publisher","first-page":"1379192","DOI":"10.3389\/fchem.2024.1379192","volume":"12","author":"T Bepler","year":"2024","unstructured":"Bepler, T. et al. Antiviral activity of the host defense peptide piscidin 1: investigating a membrane-mediated mode of action. Front. Chem. 12, 1379192. https:\/\/doi.org\/10.3389\/fchem.2024.1379192 (2024).","journal-title":"Front. Chem."},{"key":"60957_CR25","doi-asserted-by":"publisher","first-page":"e01682","DOI":"10.1128\/JVI.01682-20","volume":"94","author":"AR Hoffmann","year":"2020","unstructured":"Hoffmann, A. R. et al. Broad-Spectrum Antiviral Entry Inhibition by Interfacially Active Peptides. J. Virol. 94, e01682\u2013e01620. https:\/\/doi.org\/10.1128\/JVI.01682-20 (2020).","journal-title":"J. Virol."},{"key":"60957_CR26","doi-asserted-by":"publisher","first-page":"170526","DOI":"10.1016\/j.peptides.2021.170526","volume":"139","author":"H Heydari","year":"2021","unstructured":"Heydari, H. et al. Antiviral peptides against Coronaviridae family: A review. Peptides 139, 170526. https:\/\/doi.org\/10.1016\/j.peptides.2021.170526 (2021).","journal-title":"Peptides"},{"key":"60957_CR27","doi-asserted-by":"publisher","first-page":"117909","DOI":"10.1016\/j.bmc.2024.117909","volume":"113","author":"L Kerti","year":"2024","unstructured":"Kerti, L. & Frecer, V. Design of inhibitors of SARS-CoV-2 papain-like protease deriving from GRL0617: Structure\u2013activity relationships. Bioorg. Med. Chem. 113, 117909. https:\/\/doi.org\/10.1016\/j.bmc.2024.117909 (2024).","journal-title":"Bioorg. Med. Chem."},{"key":"60957_CR28","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/j.addr.2020.11.007","volume":"167","author":"D Sch\u00fctz","year":"2020","unstructured":"Sch\u00fctz, D. et al. Peptide and peptide-based inhibitors of SARS-CoV-2 entry. Adv. Drug Deliv Rev. 167, 47\u201365. https:\/\/doi.org\/10.1016\/j.addr.2020.11.007 (2020).","journal-title":"Adv. Drug Deliv Rev."},{"key":"60957_CR29","doi-asserted-by":"publisher","first-page":"876","DOI":"10.1021\/acs.jmedchem.1c02022","volume":"65","author":"N Liu","year":"2022","unstructured":"Liu, N. et al. Design and Evaluation of a Novel Peptide\u2013Drug Conjugate Covalently Targeting SARS-CoV-2 Papain-like Protease. J. Med. Chem. 65, 876\u2013884. https:\/\/doi.org\/10.1021\/acs.jmedchem.1c02022 (2022).","journal-title":"J. Med. Chem."},{"key":"60957_CR30","doi-asserted-by":"publisher","first-page":"e02451","DOI":"10.1128\/mBio.02451-20","volume":"11","author":"F Curreli","year":"2020","unstructured":"Curreli, F. et al. Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro. mBio 11, e02451\u2013e02420. https:\/\/doi.org\/10.1128\/mBio.02451-20 (2020).","journal-title":"mBio"},{"key":"60957_CR31","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1126\/science.abd9909","volume":"370","author":"L Cao","year":"2020","unstructured":"Cao, L. et al. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. Science 370, 426\u2013431. https:\/\/doi.org\/10.1126\/science.abd9909 (2020).","journal-title":"Science"},{"key":"60957_CR32","doi-asserted-by":"publisher","first-page":"1331","DOI":"10.1126\/science.abb4489","volume":"368","author":"W Dai","year":"2020","unstructured":"Dai, W. et al. Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease. Science 368, 1331\u20131335. https:\/\/doi.org\/10.1126\/science.abb4489 (2020).","journal-title":"Science"},{"key":"60957_CR33","doi-asserted-by":"publisher","first-page":"101053","DOI":"10.1016\/j.drup.2024.101053","volume":"73","author":"S Du","year":"2024","unstructured":"Du, S. et al. Target-based drug design strategies to overcome resistance to antiviral agents: opportunities and challenges. Drug Resist. Updat. 73, 101053. https:\/\/doi.org\/10.1016\/j.drup.2024.101053 (2024).","journal-title":"Drug Resist. Updat"},{"key":"60957_CR34","doi-asserted-by":"publisher","first-page":"2700","DOI":"10.1016\/j.bmc.2017.06.052","volume":"26","author":"JL Lau","year":"2018","unstructured":"Lau, J. L. & Dunn, M. K. Therapeutic peptides: Historical perspectives, current development trends, and future directions. Bioorg. Med. Chem. 26, 2700\u20132707. https:\/\/doi.org\/10.1016\/j.bmc.2017.06.052 (2018).","journal-title":"Bioorg. Med. Chem."},{"key":"60957_CR35","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1016\/j.drudis.2014.10.003","volume":"20","author":"K Fosgerau","year":"2015","unstructured":"Fosgerau, K. & Hoffmann, T. Peptide therapeutics: current status and future directions. Drug Discov Today. 20, 122\u2013128. https:\/\/doi.org\/10.1016\/j.drudis.2014.10.003 (2015).","journal-title":"Drug Discov Today"},{"key":"60957_CR36","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/j.antiviral.2014.12.015","volume":"115","author":"YM B\u00e1ez-Santos","year":"2015","unstructured":"B\u00e1ez-Santos, Y. M., St. John, S. E. & Mesecar, A. D. The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds. Antiviral Res. 115, 21\u201338. https:\/\/doi.org\/10.1016\/j.antiviral.2014.12.015 (2015).","journal-title":"Antiviral Res."},{"key":"60957_CR37","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1038\/s41586-020-2180-5","volume":"581","author":"J Lan","year":"2020","unstructured":"Lan, J. et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 581, 215\u2013220. https:\/\/doi.org\/10.1038\/s41586-020-2180-5 (2020).","journal-title":"Nature"},{"key":"60957_CR38","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1126\/science.abb3405","volume":"368","author":"L Zhang","year":"2020","unstructured":"Zhang, L. et al. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved \u03b1-ketoamide inhibitors. Science 368, 409\u2013412. https:\/\/doi.org\/10.1126\/science.abb3405 (2020).","journal-title":"Science"},{"key":"60957_CR39","doi-asserted-by":"publisher","first-page":"107690","DOI":"10.1016\/j.jsb.2020.107690","volume":"213","author":"M Shahid","year":"2021","unstructured":"Shahid, M. & Shahzad-ul-Hussan, S. Structural insights of key enzymes into therapeutic intervention against SARS-CoV-2. J. Struct. Biol. 213, 107690. https:\/\/doi.org\/10.1016\/j.jsb.2020.107690 (2021).","journal-title":"J. Struct. Biol."},{"key":"60957_CR40","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1093\/bioinformatics\/bty579","volume":"35","author":"Z Wen","year":"2019","unstructured":"Wen, Z., He, J., Tao, H. & Huang, S-Y. PepBDB: a comprehensive structural database of biological peptide\u2013protein interactions. Bioinformatics 35, 175\u2013177. https:\/\/doi.org\/10.1093\/bioinformatics\/bty579 (2019).","journal-title":"Bioinformatics"},{"key":"60957_CR41","doi-asserted-by":"publisher","first-page":"e0181748","DOI":"10.1371\/journal.pone.0181748","volume":"12","author":"SS Usmani","year":"2017","unstructured":"Usmani, S. S. et al. THPdb: Database of FDA-approved peptide and protein therapeutics. PLoS ONE. 12, e0181748. https:\/\/doi.org\/10.1371\/journal.pone.0181748 (2017).","journal-title":"PLOS ONE"},{"key":"60957_CR42","doi-asserted-by":"publisher","unstructured":"Blanco-M\u00edguez, A. et al. MAHMI database: a comprehensive MetaHit-based resource for the study of the mechanism of action of the human microbiota. Database 2017 baw157. https:\/\/doi.org\/10.1093\/database\/baw157 (2017).","DOI":"10.1093\/database\/baw157"},{"key":"60957_CR43","doi-asserted-by":"publisher","first-page":"e06668","DOI":"10.1016\/j.heliyon.2021.e06668","volume":"7","author":"A Chaudhary","year":"2021","unstructured":"Chaudhary, A. et al. FermFooDb: A database of bioactive peptides derived from fermented foods. Heliyon 7, e06668. https:\/\/doi.org\/10.1016\/j.heliyon.2021.e06668 (2021).","journal-title":"Heliyon"},{"key":"60957_CR44","doi-asserted-by":"publisher","first-page":"D288","DOI":"10.1093\/nar\/gkaa991","volume":"49","author":"M Pirtskhalava","year":"2021","unstructured":"Pirtskhalava, M. et al. DBAASP v3: database of antimicrobial\/cytotoxic activity and structure of peptides as a resource for development of new therapeutics. Nucleic Acids Res. 49, D288\u2013D297. https:\/\/doi.org\/10.1093\/nar\/gkaa991 (2021).","journal-title":"Nucleic Acids Res."},{"key":"60957_CR45","doi-asserted-by":"publisher","first-page":"D837","DOI":"10.1093\/nar\/gku892","volume":"43","author":"A Tyagi","year":"2015","unstructured":"Tyagi, A. et al. CancerPPD: a database of anticancer peptides and proteins. Nucleic Acids Res. 43, D837\u2013D843. https:\/\/doi.org\/10.1093\/nar\/gku892 (2015).","journal-title":"Nucleic Acids Res."},{"key":"60957_CR46","doi-asserted-by":"publisher","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","volume":"44","author":"G Wang","year":"2016","unstructured":"Wang, G., Li, X. & Wang, Z. APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 44, D1087\u2013D1093. https:\/\/doi.org\/10.1093\/nar\/gkv1278 (2016).","journal-title":"Nucleic Acids Res."},{"key":"60957_CR47","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1186\/1471-2105-10-421","volume":"10","author":"C Camacho","year":"2009","unstructured":"Camacho, C. et al. BLAST+: architecture and applications. BMC Bioinform. 10, 421. https:\/\/doi.org\/10.1186\/1471-2105-10-421 (2009).","journal-title":"BMC Bioinform."},{"key":"60957_CR48","doi-asserted-by":"publisher","unstructured":"Eswar, N. et al. Comparative protein structure modeling using modeller. Curr. Protoc. Bioinforma. 15 https:\/\/doi.org\/10.1002\/0471250953.bi0506s15 (2006).","DOI":"10.1002\/0471250953.bi0506s15"},{"key":"60957_CR49","doi-asserted-by":"publisher","first-page":"W443","DOI":"10.1093\/nar\/gky357","volume":"46","author":"P Zhou","year":"2018","unstructured":"Zhou, P., Jin, B., Li, H. & Huang, S-Y. HPEPDOCK: a web server for blind peptide\u2013protein docking based on a hierarchical algorithm. Nucleic Acids Res. 46, W443\u2013W450. https:\/\/doi.org\/10.1093\/nar\/gky357 (2018).","journal-title":"Nucleic Acids Res."},{"key":"60957_CR50","doi-asserted-by":"publisher","first-page":"7235","DOI":"10.1039\/D6CC00583G","volume":"62","author":"K Ling","year":"2026","unstructured":"Ling, K. et al. Peptide\u2013protein docking: from physics-based models to generative intelligence. Chem. Commun. 62, 7235\u20137247. https:\/\/doi.org\/10.1039\/D6CC00583G (2026).","journal-title":"Chem. Commun."},{"key":"60957_CR51","doi-asserted-by":"publisher","first-page":"108926","DOI":"10.1016\/j.compbiomed.2024.108926","volume":"179","author":"AS Rathore","year":"2024","unstructured":"Rathore, A. S. et al. ToxinPred 3.0: An improved method for predicting the toxicity of peptides. Comput. Biol. Med. 179, 108926. https:\/\/doi.org\/10.1016\/j.compbiomed.2024.108926 (2024).","journal-title":"Comput. Biol. Med."},{"key":"60957_CR52","doi-asserted-by":"publisher","first-page":"2778","DOI":"10.1021\/ci200227u","volume":"51","author":"RA Laskowski","year":"2011","unstructured":"Laskowski, R. A. & Swindells, M. B. LigPlot+: Multiple Ligand\u2013Protein Interaction Diagrams for Drug Discovery. J. Chem. Inf. Model. 51, 2778\u20132786. https:\/\/doi.org\/10.1021\/ci200227u (2011).","journal-title":"J. Chem. Inf. Model."},{"key":"60957_CR53","unstructured":"Schr\u00f6dinger, L. L. C. The PyMOL Molecular Graphics System, Version 1.8 (2015)."},{"key":"60957_CR54","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1186\/s13321-019-0362-7","volume":"11","author":"EW Bell","year":"2019","unstructured":"Bell, E. W. & Zhang, Y. DockRMSD: an open-source tool for atom mapping and RMSD calculation of symmetric molecules through graph isomorphism. J. Cheminformatics. 11, 40. https:\/\/doi.org\/10.1186\/s13321-019-0362-7 (2019).","journal-title":"J. Cheminformatics"},{"key":"60957_CR55","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/s12551-016-0247-1","volume":"9","author":"NS Pagadala","year":"2017","unstructured":"Pagadala, N. S., Syed, K. & Tuszynski, J. Software for molecular docking: a review. Biophys. Rev. 9, 91\u2013102. https:\/\/doi.org\/10.1007\/s12551-016-0247-1 (2017).","journal-title":"Biophys. Rev."},{"key":"60957_CR56","doi-asserted-by":"publisher","first-page":"5706","DOI":"10.1080\/07391102.2020.1787864","volume":"39","author":"S Sasidharan","year":"2021","unstructured":"Sasidharan, S. et al. Bacterial protein azurin and derived peptides as potential anti-SARS-CoV-2 agents: insights from molecular docking and molecular dynamics simulations. J. Biomol. Struct. Dyn. 39, 5706\u20135721. https:\/\/doi.org\/10.1080\/07391102.2020.1787864 (2021).","journal-title":"J. Biomol. Struct. Dyn."},{"key":"60957_CR57","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1126\/science.3892686","volume":"229","author":"SK Burley","year":"1985","unstructured":"Burley, S. K. & Petsko, G. A. Aromatic-Aromatic Interaction: A Mechanism of Protein Structure Stabilization. Science 229, 23\u201328. https:\/\/doi.org\/10.1126\/science.3892686 (1985).","journal-title":"Science"},{"key":"60957_CR58","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","volume":"157","author":"J Kyte","year":"1982","unstructured":"Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105\u2013132. https:\/\/doi.org\/10.1016\/0022-2836(82)90515-0 (1982).","journal-title":"J. Mol. Biol."},{"key":"60957_CR59","doi-asserted-by":"publisher","unstructured":"Abraham, M. et al. GROMACS 2024.2 Manual.  https:\/\/doi.org\/10.5281\/ZENODO.11148638 (2024).","DOI":"10.5281\/ZENODO.11148638"},{"key":"60957_CR60","doi-asserted-by":"publisher","first-page":"1545","DOI":"10.1002\/jcc.21287","volume":"30","author":"BR Brooks","year":"2009","unstructured":"Brooks, B. R. et al. CHARMM: The biomolecular simulation program. J. Comput. Chem. 30, 1545\u20131614. https:\/\/doi.org\/10.1002\/jcc.21287 (2009).","journal-title":"J. Comput. Chem."},{"key":"60957_CR61","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1021\/acs.jctc.5b00935","volume":"12","author":"J Lee","year":"2016","unstructured":"Lee, J. et al. CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM\/OpenMM Simulations Using the CHARMM36 Additive Force Field. J. Chem. Theory Comput. 12, 405\u2013413. https:\/\/doi.org\/10.1021\/acs.jctc.5b00935 (2016).","journal-title":"J. Chem. Theory Comput."},{"key":"60957_CR62","doi-asserted-by":"crossref","unstructured":"Gowers, R. et al. MD Analysis: A Python Package for the Rapid Analysis of Molecular Dynamics Simulations 98\u2013105 (Austin, 2016).","DOI":"10.25080\/Majora-629e541a-00e"},{"key":"60957_CR63","doi-asserted-by":"publisher","first-page":"2319","DOI":"10.1002\/jcc.21787","volume":"32","author":"N Michaud-Agrawal","year":"2011","unstructured":"Michaud-Agrawal, N., Denning, E. J., Woolf, T. B. & Beckstein, O. MDAnalysis: A toolkit for the analysis of molecular dynamics simulations. J. Comput. Chem. 32, 2319\u20132327. https:\/\/doi.org\/10.1002\/jcc.21787 (2011).","journal-title":"J. Comput. Chem."},{"key":"60957_CR64","doi-asserted-by":"publisher","first-page":"1637","DOI":"10.1351\/PAC-REC-10-01-02","volume":"83","author":"E Arunan","year":"2011","unstructured":"Arunan, E. et al. Definition of the hydrogen bond (IUPAC Recommendations 2011). Pure Appl. Chem. 83, 1637\u20131641. https:\/\/doi.org\/10.1351\/PAC-REC-10-01-02 (2011).","journal-title":"Pure Appl. Chem."},{"key":"60957_CR65","doi-asserted-by":"publisher","first-page":"6281","DOI":"10.1021\/acs.jctc.1c00645","volume":"17","author":"MS Vald\u00e9s-Tresanco","year":"2021","unstructured":"Vald\u00e9s-Tresanco, M. S., Vald\u00e9s-Tresanco, M. E., Valiente, P. A. & Moreno, E. gmx_MMPBSA: A New Tool to Perform End-State Free Energy Calculations with GROMACS. J. Chem. Theory Comput. 17, 6281\u20136291. https:\/\/doi.org\/10.1021\/acs.jctc.1c00645 (2021).","journal-title":"J. Chem. Theory Comput."},{"key":"60957_CR66","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1186\/s13321-019-0330-2","volume":"11","author":"PW Kenny","year":"2019","unstructured":"Kenny, P. W. The nature of ligand efficiency. J. Cheminformatics. 11, 8. https:\/\/doi.org\/10.1186\/s13321-019-0330-2 (2019).","journal-title":"J. Cheminformatics"},{"key":"60957_CR67","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1517\/17460441.2015.1032936","volume":"10","author":"S Genheden","year":"2015","unstructured":"Genheden, S. & Ryde, U. The MM\/PBSA and MM\/GBSA methods to estimate ligand-binding affinities. Expert Opin. Drug Discov. 10, 449\u2013461. https:\/\/doi.org\/10.1517\/17460441.2015.1032936 (2015).","journal-title":"Expert Opin. Drug Discov"},{"key":"60957_CR68","doi-asserted-by":"publisher","first-page":"6127","DOI":"10.1021\/acs.jctc.8b00391","volume":"14","author":"B Knapp","year":"2018","unstructured":"Knapp, B., Ospina, L. & Deane, C. M. Avoiding False Positive Conclusions in Molecular Simulation: The Importance of Replicas. J. Chem. Theory Comput. 14, 6127\u20136138. https:\/\/doi.org\/10.1021\/acs.jctc.8b00391 (2018).","journal-title":"J. Chem. Theory Comput."},{"key":"60957_CR69","doi-asserted-by":"publisher","DOI":"10.33011\/livecoms.1.1.5067","author":"A Grossfield","year":"2019","unstructured":"Grossfield, A. et al. Best Practices for Quantification of Uncertainty and Sampling Quality in Molecular Simulations [Article v1.0]. Living J. Comput. Mol. Sci. https:\/\/doi.org\/10.33011\/livecoms.1.1.5067 (2019). 1:.","journal-title":"Living J. Comput. Mol. Sci."},{"key":"60957_CR70","doi-asserted-by":"publisher","unstructured":"Zakaryan, H. et al. Natural antimicrobial peptides as a source of new antiviral agents. J. Gen. Virol. 102 https:\/\/doi.org\/10.1099\/jgv.0.001661 (2021).","DOI":"10.1099\/jgv.0.001661"},{"key":"60957_CR71","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1615\/CritRevTherDrugCarrierSyst.2022040322","volume":"40","author":"R Thakur","year":"2023","unstructured":"Thakur, R., Suri, C. R., Kaur, I. P. & Rishi, P. Peptides as Diagnostic, Therapeutic, and Theranostic Tools: Progress and Future Challenges. Crit. Rev. Ther. Drug Carr. Syst. 40, 49\u2013100. https:\/\/doi.org\/10.1615\/CritRevTherDrugCarrierSyst.2022040322 (2023).","journal-title":"Crit. Rev. Ther. Drug Carr. Syst."},{"key":"60957_CR72","doi-asserted-by":"publisher","first-page":"2940","DOI":"10.1021\/acs.jmedchem.1c01307","volume":"65","author":"Z Shen","year":"2022","unstructured":"Shen, Z. et al. Design of SARS-CoV-2 PLpro Inhibitors for COVID-19 Antiviral Therapy Leveraging Binding Cooperativity. J. Med. Chem. 65, 2940\u20132955. https:\/\/doi.org\/10.1021\/acs.jmedchem.1c01307 (2022).","journal-title":"J. Med. Chem."},{"key":"60957_CR73","doi-asserted-by":"publisher","first-page":"1844","DOI":"10.1016\/j.bbagen.2017.03.024","volume":"1861","author":"M Bacalum","year":"2017","unstructured":"Bacalum, M. et al. Modulating short tryptophan- and arginine-rich peptides activity by substitution with histidine. Biochim. Biophys. Acta BBA Gen. Subj. 1861, 1844\u20131854. https:\/\/doi.org\/10.1016\/j.bbagen.2017.03.024 (2017).","journal-title":"Biochim. Biophys. Acta BBA - Gen. Subj."},{"key":"60957_CR74","doi-asserted-by":"publisher","unstructured":"Bolosov, I. A. et al. Design of protegrin-1 analogs with improved antibacterial selectivity. Pharmaceutics 15, 2047. https:\/\/doi.org\/10.3390\/pharmaceutics15082047 (2023).","DOI":"10.3390\/pharmaceutics15082047"},{"key":"60957_CR75","doi-asserted-by":"publisher","first-page":"106205","DOI":"10.1016\/j.ejps.2022.106205","volume":"175","author":"HJ Park","year":"2022","unstructured":"Park, H. J. et al. Bactericidal activities and action mechanism of the novel antimicrobial peptide Hylin a1 and its analog peptides against Acinetobacter baumannii infection. Eur. J. Pharm. Sci. 175, 106205. https:\/\/doi.org\/10.1016\/j.ejps.2022.106205 (2022).","journal-title":"Eur. J. Pharm. Sci."},{"key":"60957_CR76","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1038\/s42003-018-0224-2","volume":"1","author":"MDT Torres","year":"2018","unstructured":"Torres, M. D. T. et al. Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates. Commun. Biol. 1, 221. https:\/\/doi.org\/10.1038\/s42003-018-0224-2 (2018).","journal-title":"Commun. Biol."},{"key":"60957_CR77","doi-asserted-by":"publisher","first-page":"14602","DOI":"10.1038\/s41598-018-32981-3","volume":"8","author":"C-H Yang","year":"2018","unstructured":"Yang, C-H. et al. An engineered arginine-rich \u03b1-helical antimicrobial peptide exhibits broad-spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice. Sci. Rep. 8, 14602. https:\/\/doi.org\/10.1038\/s41598-018-32981-3 (2018).","journal-title":"Sci. Rep."},{"key":"60957_CR78","doi-asserted-by":"publisher","first-page":"e2317747121","DOI":"10.1073\/pnas.2317747121","volume":"121","author":"O Stenstr\u00f6m","year":"2024","unstructured":"Stenstr\u00f6m, O., Diehl, C., Modig, K. & Akke, M. Ligand-induced protein transition state stabilization switches the binding pathway from conformational selection to induced fit. Proc. Natl. Acad. Sci. 121, e2317747121. https:\/\/doi.org\/10.1073\/pnas.2317747121 (2024).","journal-title":"Proc. Natl. Acad. Sci."},{"key":"60957_CR79","doi-asserted-by":"publisher","first-page":"e59627","DOI":"10.1371\/journal.pone.0059627","volume":"8","author":"Q Yu","year":"2013","unstructured":"Yu, Q., Ye, W., Wang, W. & Chen, H-F. Global Conformational Selection and Local Induced Fit for the Recognition between Intrinsic Disordered p53 and CBP. PLoS ONE. 8, e59627. https:\/\/doi.org\/10.1371\/journal.pone.0059627 (2013).","journal-title":"PLoS ONE"},{"key":"60957_CR80","doi-asserted-by":"publisher","unstructured":"Gelpi, J., Hospital, A., Go\u00f1i, R. & Orozco, M. Molecular dynamics simulations: advances and applications. Adv. Appl. Bioinforma Chem. 37 https:\/\/doi.org\/10.2147\/AABC.S70333 (2015).","DOI":"10.2147\/AABC.S70333"},{"key":"60957_CR81","doi-asserted-by":"publisher","first-page":"40040","DOI":"10.1038\/s41598-025-23842-x","volume":"15","author":"M Dabbagh Hosseini Pour","year":"2025","unstructured":"Dabbagh Hosseini Pour, M., Jahanbin Sardroodi, J., Hadidi, N. & Pazuki, G. Detailed atomistic investigation of aggregation and interaction of teriparatide in aqueous media. Sci. Rep. 15, 40040. https:\/\/doi.org\/10.1038\/s41598-025-23842-x (2025).","journal-title":"Sci. Rep."},{"key":"60957_CR82","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.crstbi.2020.11.002","volume":"3","author":"KP Tan","year":"2021","unstructured":"Tan, K. P., Singh, K., Hazra, A. & Madhusudhan, M. S. Peptide bond planarity constrains hydrogen bond geometry and influences secondary structure conformations. Curr. Res. Struct. Biol. 3, 1\u20138. https:\/\/doi.org\/10.1016\/j.crstbi.2020.11.002 (2021).","journal-title":"Curr. Res. Struct. Biol."},{"key":"60957_CR83","doi-asserted-by":"publisher","first-page":"348","DOI":"10.1007\/s42452-026-08368-9","volume":"8","author":"BY Alhatlani","year":"2026","unstructured":"Alhatlani, B. Y. et al. Integrated in silico approach identifies Chrysosplenol D from Artemisia annua as a potent candidate against SARS-CoV-2, MERS-CoV, and HSV-2 proteases. Discov Appl. Sci. 8, 348. https:\/\/doi.org\/10.1007\/s42452-026-08368-9 (2026).","journal-title":"Discov Appl. Sci."},{"key":"60957_CR84","doi-asserted-by":"publisher","first-page":"25908","DOI":"10.1039\/D4RA03877K","volume":"14","author":"Y Guo","year":"2024","unstructured":"Guo, Y. et al. Molecular insight into binding affinities and blockade effects of selected flavonoid compounds on the PD-1\/PD-L1 pathway. RSC Adv. 14, 25908\u201325917. https:\/\/doi.org\/10.1039\/D4RA03877K (2024).","journal-title":"RSC Adv."},{"key":"60957_CR85","doi-asserted-by":"publisher","first-page":"3305","DOI":"10.3390\/math13203305","volume":"13","author":"P Kang","year":"2025","unstructured":"Kang, P. Evaluation of GPU-Accelerated Edge Platforms for Stochastic Simulations: Performance and Energy Efficiency Analysis. Mathematics 13, 3305. https:\/\/doi.org\/10.3390\/math13203305 (2025).","journal-title":"Mathematics"},{"key":"60957_CR86","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","volume":"1\u20132","author":"MJ Abraham","year":"2015","unstructured":"Abraham, M. J. et al. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1\u20132, 19\u201325. https:\/\/doi.org\/10.1016\/j.softx.2015.06.001 (2015).","journal-title":"SoftwareX"},{"key":"60957_CR87","doi-asserted-by":"publisher","first-page":"5792","DOI":"10.1021\/acs.jctc.2c00585","volume":"18","author":"S Kieninger","year":"2022","unstructured":"Kieninger, S. & Keller, B. G. GROMACS Stochastic Dynamics and BAOAB Are Equivalent Configurational Sampling Algorithms. J. Chem. Theory Comput. 18, 5792\u20135798. https:\/\/doi.org\/10.1021\/acs.jctc.2c00585 (2022).","journal-title":"J. Chem. Theory Comput."},{"key":"60957_CR88","doi-asserted-by":"publisher","first-page":"6993","DOI":"10.1039\/D0SM00736F","volume":"16","author":"AN Rissanou","year":"2020","unstructured":"Rissanou, A. N., Ouranidis, A. & Karatasos, K. Complexation of single stranded RNA with an ionizable lipid: an all-atom molecular dynamics simulation study. Soft Matter. 16, 6993\u20137005. https:\/\/doi.org\/10.1039\/D0SM00736F (2020).","journal-title":"Soft Matter"},{"key":"60957_CR89","doi-asserted-by":"publisher","first-page":"5988","DOI":"10.3390\/molecules27185988","volume":"27","author":"WS Qayed","year":"2022","unstructured":"Qayed, W. S., Ferreira, R. S. & Silva, J. R. A. In Silico Study towards Repositioning of FDA-Approved Drug Candidates for Anticoronaviral Therapy: Molecular Docking, Molecular Dynamics and Binding Free Energy Calculations. Molecules 27, 5988. https:\/\/doi.org\/10.3390\/molecules27185988 (2022).","journal-title":"Molecules"},{"key":"60957_CR90","doi-asserted-by":"publisher","first-page":"1183","DOI":"10.1261\/rna.065896.118","volume":"24","author":"F Chen","year":"2018","unstructured":"Chen, F. et al. Assessing the performance of MM\/PBSA and MM\/GBSA methods. 8. Predicting binding free energies and poses of protein\u2013RNA complexes. RNA 24, 1183\u20131194. https:\/\/doi.org\/10.1261\/rna.065896.118 (2018).","journal-title":"RNA"},{"key":"60957_CR91","doi-asserted-by":"publisher","first-page":"e3558","DOI":"10.1002\/psc.3558","volume":"30","author":"A Falanga","year":"2024","unstructured":"Falanga, A., Bellavita, R., Braccia, S. & Galdiero, S. Hydrophobicity: The door to drug delivery. J. Pept. Sci. 30, e3558. https:\/\/doi.org\/10.1002\/psc.3558 (2024).","journal-title":"J. Pept. Sci."},{"key":"60957_CR92","doi-asserted-by":"publisher","first-page":"103366","DOI":"10.1016\/j.drudis.2022.103366","volume":"27","author":"P Agarwal","year":"2022","unstructured":"Agarwal, P., Huckle, J., Newman, J. & Reid, D. L. Trends in small molecule drug properties: A developability molecule assessment perspective. Drug Discov Today. 27, 103366. https:\/\/doi.org\/10.1016\/j.drudis.2022.103366 (2022).","journal-title":"Drug Discov Today"},{"key":"60957_CR93","doi-asserted-by":"publisher","first-page":"14977","DOI":"10.1039\/D4SC02758B","volume":"15","author":"MP Thorpe","year":"2024","unstructured":"Thorpe, M. P. et al. The backbone constitution drives passive permeability independent of side chains in depsipeptide and peptide macrocycles inspired by ent -verticilide. Chem. Sci. 15, 14977\u201314987. https:\/\/doi.org\/10.1039\/D4SC02758B (2024).","journal-title":"Chem. Sci."},{"key":"60957_CR94","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.jmgm.2015.09.010","volume":"62","author":"S Kassem","year":"2015","unstructured":"Kassem, S., Ahmed, M., El-Sheikh, S. & Barakat, K. H. Entropy in bimolecular simulations: A comprehensive review of atomic fluctuations-based methods. J. Mol. Graph Model. 62, 105\u2013117. https:\/\/doi.org\/10.1016\/j.jmgm.2015.09.010 (2015).","journal-title":"J. Mol. Graph Model."},{"key":"60957_CR95","doi-asserted-by":"publisher","first-page":"9478","DOI":"10.1021\/acs.chemrev.9b00055","volume":"119","author":"E Wang","year":"2019","unstructured":"Wang, E. et al. End-Point Binding Free Energy Calculation with MM\/PBSA and MM\/GBSA: Strategies and Applications in Drug Design. Chem. Rev. 119, 9478\u20139508. https:\/\/doi.org\/10.1021\/acs.chemrev.9b00055 (2019).","journal-title":"Chem. Rev."},{"key":"60957_CR96","doi-asserted-by":"publisher","first-page":"6017","DOI":"10.1038\/s41598-019-41758-1","volume":"9","author":"DW Wright","year":"2019","unstructured":"Wright, D. W. et al. Application of ESMACS binding free energy protocols to diverse datasets: Bromodomain-containing protein 4. Sci. Rep. 9, 6017. https:\/\/doi.org\/10.1038\/s41598-019-41758-1 (2019).","journal-title":"Sci. Rep."},{"key":"60957_CR97","doi-asserted-by":"publisher","first-page":"105346","DOI":"10.1016\/j.jbc.2023.105346","volume":"299","author":"M Yang","year":"2023","unstructured":"Yang, M. et al. SARS-CoV-2 papain-like protease plays multiple roles in regulating cellular proteins in the endoplasmic reticulum. J. Biol. Chem. 299, 105346. https:\/\/doi.org\/10.1016\/j.jbc.2023.105346 (2023).","journal-title":"J. Biol. Chem."},{"key":"60957_CR98","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1016\/j.tips.2017.01.003","volume":"38","author":"G Guidotti","year":"2017","unstructured":"Guidotti, G., Brambilla, L. & Rossi, D. Cell-Penetrating Peptides: From Basic Research to Clinics. Trends Pharmacol. Sci. 38, 406\u2013424. https:\/\/doi.org\/10.1016\/j.tips.2017.01.003 (2017).","journal-title":"Trends Pharmacol. Sci."},{"key":"60957_CR99","doi-asserted-by":"publisher","first-page":"106630","DOI":"10.1016\/j.ejps.2023.106630","volume":"192","author":"D Luo","year":"2024","unstructured":"Luo, D. et al. A comprehensive review of advanced nasal delivery: Specially insulin and calcitonin. Eur. J. Pharm. Sci. 192, 106630. https:\/\/doi.org\/10.1016\/j.ejps.2023.106630 (2024).","journal-title":"Eur. J. Pharm. Sci."},{"key":"60957_CR100","doi-asserted-by":"publisher","first-page":"1068495","DOI":"10.3389\/fphar.2022.1068495","volume":"13","author":"J Maeng","year":"2022","unstructured":"Maeng, J. & Lee, K. Systemic and brain delivery of antidiabetic peptides through nasal administration using cell-penetrating peptides. Front. Pharmacol. 13, 1068495. https:\/\/doi.org\/10.3389\/fphar.2022.1068495 (2022).","journal-title":"Front. Pharmacol."},{"key":"60957_CR101","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1016\/j.jconrel.2012.01.024","volume":"161","author":"L Illum","year":"2012","unstructured":"Illum, L. Nasal drug delivery \u2014 Recent developments and future prospects. J. Controlled Release. 161, 254\u2013263. https:\/\/doi.org\/10.1016\/j.jconrel.2012.01.024 (2012).","journal-title":"J. Controlled Release"},{"key":"60957_CR102","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1038\/s41392-022-00904-4","volume":"7","author":"L Wang","year":"2022","unstructured":"Wang, L. et al. Therapeutic peptides: current applications and future directions. Signal. Transduct. Target. Ther. 7, 48. https:\/\/doi.org\/10.1038\/s41392-022-00904-4 (2022).","journal-title":"Signal. Transduct. Target. Ther."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-60957-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-60957-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-60957-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T09:50:47Z","timestamp":1788515447000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-60957-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,4]]},"references-count":102,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["60957"],"URL":"https:\/\/doi.org\/10.1038\/s41598-026-60957-1","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,4]]},"assertion":[{"value":"12 February 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"1 July 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 September 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"27791"}}