{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T11:29:44Z","timestamp":1790767784292,"version":"4.1.0"},"reference-count":51,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2021,3,31]],"date-time":"2021-03-31T00:00:00Z","timestamp":1617148800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1DP1 OD029517-01"],"award-info":[{"award-number":["1DP1 OD029517-01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>Viral infections, such as those caused by Herpes Simplex Virus-1 (HSV-1) and SARS-CoV-2, affect millions of people each year. However, there are few antiviral drugs that can effectively treat these infections. The standard approach in the development of antiviral drugs involves the identification of a unique viral target, followed by the design of an agent that addresses that target. Antimicrobial peptides (AMPs) represent a novel source of potential antiviral drugs. AMPs have been shown to inactivate numerous different enveloped viruses through the disruption of their viral envelopes. However, the clinical development of AMPs as antimicrobial therapeutics has been hampered by a number of factors, especially their enzymatically labile structure as peptides. We have examined the antiviral potential of peptoid mimics of AMPs (sequence-specific N-substituted glycine oligomers). These peptoids have the distinct advantage of being insensitive to proteases, and also exhibit increased bioavailability and stability. Our results demonstrate that several peptoids exhibit potent in vitro antiviral activity against both HSV-1 and SARS-CoV-2 when incubated prior to infection. In other words, they have a direct effect on the viral structure, which appears to render the viral particles non-infective. Visualization by cryo-EM shows viral envelope disruption similar to what has been observed with AMP activity against other viruses. Furthermore, we observed no cytotoxicity against primary cultures of oral epithelial cells. These results suggest a common or biomimetic mechanism, possibly due to the differences between the phospholipid head group makeup of viral envelopes and host cell membranes, thus underscoring the potential of this class of molecules as safe and effective broad-spectrum antiviral agents. We discuss how and why differing molecular features between 10 peptoid candidates may affect both antiviral activity and selectivity.<\/jats:p>","DOI":"10.3390\/ph14040304","type":"journal-article","created":{"date-parts":[[2021,3,31]],"date-time":"2021-03-31T05:57:18Z","timestamp":1617170238000},"page":"304","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":52,"title":["Potent Antiviral Activity against HSV-1 and SARS-CoV-2 by Antimicrobial Peptoids"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3596-9773","authenticated-orcid":false,"given":"Gill","family":"Diamond","sequence":"first","affiliation":[{"name":"Department of Oral Immunology and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY 40202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Molchanova","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Stanford University School of Medicine, Stanford, CA 94305, USA"},{"name":"Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudine","family":"Herlan","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Stanford University School of Medicine, Stanford, CA 94305, USA"},{"name":"Institute of Organic Chemistry, Karlsruhe Institute of Technology, 76131 Karlsruhe, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Fortkort","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Stanford University School of Medicine, Stanford, CA 94305, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer","family":"Lin","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Stanford University School of Medicine, Stanford, CA 94305, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erika","family":"Figgins","sequence":"additional","affiliation":[{"name":"Department of Oral Immunology and Infectious Diseases, University of Louisville School of Dentistry, Louisville, KY 40202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathen","family":"Bopp","sequence":"additional","affiliation":[{"name":"Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6422-7720","authenticated-orcid":false,"given":"Lisa","family":"Ryan","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases and Global Medicine, Department of Medicine, University of Florida School of Medicine, Gainesville, FL 32601, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donghoon","family":"Chung","sequence":"additional","affiliation":[{"name":"Center for Predictive Medicine, Department of Microbiology, School of Medicine, University of Louisville, Louisville, KY 40202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Adcock","sequence":"additional","affiliation":[{"name":"Center for Predictive Medicine, Department of Microbiology, School of Medicine, University of Louisville, Louisville, KY 40202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3680-8066","authenticated-orcid":false,"given":"Michael","family":"Sherman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0735-6873","authenticated-orcid":false,"given":"Annelise","family":"Barron","sequence":"additional","affiliation":[{"name":"Department of Bioengineering, Stanford University School of Medicine, Stanford, CA 94305, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,3,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1542\/pir.30.4.119","article-title":"Herpes simplex","volume":"30","author":"Chayavichitsilp","year":"2009","journal-title":"Pediatr. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3389\/fnagi.2018.00048","article-title":"Molecular Mechanisms for Herpes Simplex Virus Type 1 Pathogenesis in Alzheimer\u2019s Disease","volume":"10","author":"Harris","year":"2018","journal-title":"Front. Aging. Neurosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1111\/j.1600-0714.2007.00586.x","article-title":"Herpes Simplex Virus Type 1 infection: Overview on relevant clinico-pathological features","volume":"37","author":"Arduino","year":"2008","journal-title":"J. Oral Pathol. Med."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1093\/infdis\/161.2.185","article-title":"Treatment of recurrent herpes simplex labialis with oral acyclovir","volume":"161","author":"Spruance","year":"1990","journal-title":"J. Infect. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1128\/AAC.00615-10","article-title":"Resistance of herpes simplex viruses to nucleoside analogues: Mechanisms, prevalence, and management","volume":"55","author":"Piret","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1034\/j.1600-065X.2000.917304.x","article-title":"The Innate Immune Response of the Respiratory Epithelium","volume":"173","author":"Diamond","year":"2000","journal-title":"Immunol. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Brice, D.C., and Diamond, G. (2020). Antiviral Activities of Human Host Defense Peptides. Curr. Med. Chem.","DOI":"10.2174\/0929867326666190805151654"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.antiviral.2018.07.025","article-title":"LL-37 disrupts the Kaposi\u2019s sarcoma-associated herpesvirus envelope and inhibits infection in oral epithelial cells","volume":"158","author":"Brice","year":"2018","journal-title":"Antivir. Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1159\/000491497","article-title":"Design and Assessment of Anti-Biofilm Peptides: Steps Toward Clinical Application","volume":"11","author":"Dostert","year":"2019","journal-title":"J. Innate. Immun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2016.00194","article-title":"Antimicrobial Peptides: An Emerging Category of Therapeutic Agents","volume":"6","author":"Mahlapuu","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1021\/acs.jmedchem.7b00318","article-title":"The Current State of Peptide Drug Discovery: Back to the Future?","volume":"61","author":"Henninot","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.chembiol.2015.01.002","article-title":"D-enantiomeric peptides that eradicate wild-type and multidrug-resistant biofilms and protect against lethal Pseudomonas aeruginosa infections","volume":"22","author":"Reffuveille","year":"2015","journal-title":"Chem. Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/0014-5793(90)81351-N","article-title":"All-D-magainin: Chirality, antimicrobial activity and proteolytic resistance","volume":"274","author":"Bessalle","year":"1990","journal-title":"FEBS Lett."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/ph8030366","article-title":"Peptides and Peptidomimetics for Antimicrobial Drug Design","volume":"8","author":"Mojsoska","year":"2015","journal-title":"Pharmaceuticals"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/S1367-5931(02)00385-X","article-title":"Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers","volume":"6","author":"Patch","year":"2002","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_16","first-page":"885","article-title":"Pharmacologic characterization of CHIR 2279, an N-substituted glycine peptoid with high-affinity binding for alpha 1-adrenoceptors","volume":"277","author":"Gibbons","year":"1996","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1002\/ddr.430350105","article-title":"Comparison of the proteolytic susceptibilites of homologous L-amino acid, D-amino acid, and N-substituted glycine peptide and peptoid oligomers","volume":"35","author":"Miller","year":"1995","journal-title":"Drug Dev. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1002\/bip.1058","article-title":"Extreme stability of helices formed by water-soluble poly-N-substituted glycines (polypeptoids) with alpha-chiral side chains","volume":"63","author":"Sanborn","year":"2002","journal-title":"Biopolymers"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2958","DOI":"10.1021\/ja003153v","article-title":"Peptoid oligomers with alpha-chiral, aromatic side chains: Effects of chain length on secondary structure","volume":"123","author":"Wu","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4303","DOI":"10.1073\/pnas.95.8.4303","article-title":"Sequence-specific polypeptoids: A diverse family of heteropolymers with stable secondary structure","volume":"95","author":"Kirshenbaum","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"10646","DOI":"10.1021\/ja00052a076","article-title":"Efficient method for the preparation of peptoids [oligo (N-substituted glycines)] by submonomer solid-phase synthesis","volume":"114","author":"Zuckermann","year":"1992","journal-title":"J. Am. Chem. Soc."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1002\/aic.11402","article-title":"Protein and peptide biomimicry: Gold-mining inspiration from Nature\u2019s ingenuity","volume":"54","author":"Czyzewski","year":"2007","journal-title":"AIChE J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2794","DOI":"10.1073\/pnas.0708254105","article-title":"Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides","volume":"105","author":"Chongsiriwatana","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5399","DOI":"10.1128\/AAC.00578-11","article-title":"Functional synergy between antimicrobial peptoids and peptides against Gram-negative bacteria","volume":"55","author":"Chongsiriwatana","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Czyzewski, A.M., Jenssen, H., Fjell, C.D., Waldbrook, M., Chongsiriwatana, N.P., Yuen, E., Hancock, R.E., and Barron, A.E. (2016). In Vivo, In Vitro, and In Silico Characterization of Peptoids as Antimicrobial Agents. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0135961"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s10989-008-9136-1","article-title":"A VEGFR2 Antagonist and Other Peptoids Evade Immune Recognition","volume":"14","author":"Astle","year":"2008","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"12092","DOI":"10.1021\/ja037320d","article-title":"Helical peptoid mimics of magainin-2 amide","volume":"125","author":"Patch","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"19375","DOI":"10.1073\/pnas.0906145106","article-title":"Soft X-ray tomography of phenotypic switching and the cellular response to antifungal peptoids in Candida albicans","volume":"106","author":"Uchida","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3054","DOI":"10.1128\/AAC.01516-10","article-title":"Antimicrobial peptoids are effective against Pseudomonas aeruginosa biofilms","volume":"55","author":"Kapoor","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"16718","DOI":"10.1038\/s41598-017-16180-0","article-title":"Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids","volume":"7","author":"Chongsiriwatana","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1128\/AAC.01080-10","article-title":"Short alkylated peptoid mimics of antimicrobial lipopeptides","volume":"55","author":"Chongsiriwatana","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3058","DOI":"10.1128\/AAC.01667-10","article-title":"Efficacy of antimicrobial peptoids against Mycobacterium tuberculosis","volume":"55","author":"Kapoor","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_33","unstructured":"Barron, A.E. (2020, January 16\u201320). Biomimetic Drugs: In Vitro, In Vivo And Mechanistic Studies of 5-12mer Antimicrobial & Antiviral Peptoids to Treat Respiratory Infections at the Airway Interface. Proceedings of the Virtual AIChE Annual Meeting, New York, NY, USA."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"14805","DOI":"10.1038\/s41598-020-71771-8","article-title":"Halogenation as a tool to tune antimicrobial activity of peptoids","volume":"10","author":"Molchanova","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"7918","DOI":"10.1128\/JVI.00645-06","article-title":"Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy","volume":"80","author":"Neuman","year":"2006","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1080\/02713680590934111","article-title":"Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity","volume":"30","author":"Gordon","year":"2005","journal-title":"Curr. Eye Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"635","DOI":"10.2217\/fmb.11.27","article-title":"Road to clinical efficacy: Challenges and novel strategies for antimicrobial peptide development","volume":"6","author":"Eckert","year":"2011","journal-title":"Future Microbiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/j.coph.2006.04.006","article-title":"Antibacterial peptides for therapeutic use: Obstacles and realistic outlook","volume":"6","author":"Marr","year":"2006","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.2174\/1568026620999200517043137","article-title":"Novel Drugs Targeting the SARS-CoV-2\/COVID-19 Machinery","volume":"20","author":"Sternberg","year":"2020","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Roy, M., Lebeau, L., Chessa, C., Damour, A., Ladram, A., Oury, B., Boutolleau, D., Bodet, C., and Leveque, N. (2019). Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [K (3)] SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1. Viruses, 11.","DOI":"10.3390\/v11010077"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3157","DOI":"10.1073\/pnas.0909587107","article-title":"A broad-spectrum antiviral targeting entry of enveloped viruses","volume":"107","author":"Wolf","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.tibtech.2011.05.001","article-title":"The expanding scope of antimicrobial peptide structures and their modes of action","volume":"29","author":"Nguyen","year":"2011","journal-title":"Trends Biotechnol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1006\/viro.1994.1252","article-title":"The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei","volume":"200","author":"Brandimarti","year":"1994","journal-title":"Virology"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nrmicro3469","article-title":"Viral apoptotic mimicry","volume":"13","author":"Amara","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Luteijn, R.D., Praest, P., Thiele, F., Sadasivam, S.M., Singethan, K., Drijfhout, J.W., Bach, C., de Boer, S.M., Lebbink, R.J., and Tao, S. (2020). A Broad-Spectrum Antiviral Peptide Blocks Infection of Viruses by Binding to Phosphatidylserine in the Viral Envelope. Cells, 9.","DOI":"10.3390\/cells9091989"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4503","DOI":"10.1002\/chem.200501202","article-title":"Formation of RACK-and grid-type metallosupramolecular architectures and generation of moleculare motion by reversible uncoiling of helical ligand strands","volume":"12","author":"Stadler","year":"2006","journal-title":"Chemistry"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Roth, A., Lutke, S., Meinberger, D., Hermes, G., Sengle, G., Koch, M., Streichert, T., and Klatt, A.R. (2020). LL-37 fights SARS-CoV-2: The Vitamin D-Inducible Peptide LL-37 Inhibits Binding of SARS-CoV-2 Spike Protein to its Cellular Receptor Angiotensin Converting Enzyme 2 In Vitro. bioRxiv.","DOI":"10.1101\/2020.12.02.408153"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1189\/jlb.0209079","article-title":"Modulation of human {beta}-defensin-1 (hBD-1) in plasmacytoid dendritic cells (PDC), monocytes, and epithelial cells by influenza virus, Herpes simplex virus, and Sendai virus and its possible role in innate immunity","volume":"90","author":"Ryan","year":"2011","journal-title":"J. Leukoc. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Martins, W.K. (2009). A useful procedure to isolate simulateneously DNA and RNA from a single tumor sample. Protoc. Exch.","DOI":"10.1038\/nprot.2009.163"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e01439-19","DOI":"10.1128\/JVI.01439-19","article-title":"Near-Atomic-Resolution Cryo-Electron Microscopy Structures of Cucumber Leaf Spot Virus and Red Clover Necrotic Mosaic Virus: Evolutionary Divergence at the Icosahedral Three-Fold Axes","volume":"94","author":"Sherman","year":"2020","journal-title":"J. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"9775","DOI":"10.1128\/JVI.00876-10","article-title":"Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy","volume":"84","author":"Sherman","year":"2010","journal-title":"J. Virol."}],"container-title":["Pharmaceuticals"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1424-8247\/14\/4\/304\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,13]],"date-time":"2025-10-13T14:10:44Z","timestamp":1760364644000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1424-8247\/14\/4\/304"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,3,31]]},"references-count":51,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2021,4]]}},"alternative-id":["ph14040304"],"URL":"https:\/\/doi.org\/10.3390\/ph14040304","relation":{"has-preprint":[{"id-type":"doi","id":"10.20944\/preprints202103.0258.v1","asserted-by":"object"}]},"ISSN":["1424-8247"],"issn-type":[{"value":"1424-8247","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,3,31]]}}}