Molecular dynamic simulation reveals spider antimicrobial peptide Latarcin-1 and human eosinophil cationic protein as peptide inhibitors of SARS-CoV-2 variants
COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind recept...
Saved in:
Published in | Journal of biomolecular structure & dynamics Vol. 42; no. 11; pp. 5858 - 5868 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Taylor & Francis
23.07.2024
|
Subjects | |
Online Access | Get full text |
ISSN | 0739-1102 1538-0254 1538-0254 |
DOI | 10.1080/07391102.2023.2274514 |
Cover
Abstract | COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors.
Communicated by Ramaswamy H. Sarma |
---|---|
AbstractList | COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors.Communicated by Ramaswamy H. Sarma. COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors.Communicated by Ramaswamy H. Sarma.COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors.Communicated by Ramaswamy H. Sarma. COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block SARS-CoV-2 infection. The investigation focuses on the crucial host receptors angiotensin-converting enzyme 2 (ACE2) , which can bind receptor-binding domain (RBD) on the SARS-CoV-2 spike protein (S). To investigate the inhibitory effects of human Eosinophil Cationic Protein (hECP) and Latarcin-1 (L1)on SARS-CoV-2 infection, we have selected them as research subjects. Further, we ran extensive molecular dynamics simulations to bring the docked peptide-ACE2 complex into its equilibrium state. The outcomes were then evaluated with g_MMPBSA and interaction analysis. We have also considered the Delta and Omicron variants to examine these peptides' inhibitory effects. The experimental findings revealed an enhanced capability of L1 and hECP as SARS-CoV-2 inhibitors, occupying hot spots and numerous key residues in ACE2. These include ASP30, ASP38, GLU35 and GLU75, which significantly inhibit the binding of RBD and ACE2 and are effective against two common variants in a similar manner. In addition, this study can serve as a springboard for future research on SARS-CoV-2 inhibitors. Communicated by Ramaswamy H. Sarma |
Author | Mehmood, Aamir Li, Daixi Cao, Cheng |
Author_xml | – sequence: 1 givenname: Cheng surname: Cao fullname: Cao, Cheng organization: AI Research Center, Peng Cheng Laboratory, Shenzhen, Guangdong – sequence: 2 givenname: Aamir surname: Mehmood fullname: Mehmood, Aamir organization: State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai – sequence: 3 givenname: Daixi surname: Li fullname: Li, Daixi organization: AI Research Center, Peng Cheng Laboratory, Shenzhen, Guangdong |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37938133$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kc1u1DAUhS1URKeFRwB5ySaDf5JJvKMaQYs0CIkCW-vaudEYOXawk6J5Gl4VDzPtkpV1re-ce3XOFbkIMSAhrzlbc9axd6yVinMm1oIJuRairRtePyMr3siuYqKpL8jqyFRH6JJc5fyTMcF5y1-QS9kq2XEpV-TP5-jRLh4S7Q8BRmdpdmOZZxcDTfiA4DPNk-sxUQizK0SKxoGnE05z-aY7mCFZFypegJ7ulxECxZhdiNPeeWr_eRXjKcUZXaCQn7Qu7J1xc0yZxoHe33y9r7bxRyXoAyRX1uWX5PlQLsBX5_eafP_44dv2rtp9uf20vdlVVvJ6rpSyoIyyTWOFsVCrXrVGWpTNRjHsaotGqn4jW8kHqAfBGAIYhcZahSVHeU3ennzLkb8WzLMeXbboPQSMS9ai69q63ZRcC_rmjC5mxF5PyY2QDvox1AI0J6AklXPC4QnhTB_L04_l6WN5-lxe0b0_6VwYYhrhd0y-1zMcfExDgmBd1vL_Fn8B-G-jZA |
Cites_doi | 10.1038/s41421-020-00231-4 10.1007/s12539-021-00477-w 10.1186/s40001-022-00647-6 10.1016/j.ajpath.2021.10.019 10.1016/j.bbrc.2020.11.021 10.1101/2020.03.17.20037432 10.1136/bmj.n771 10.1021/ci500020m 10.1039/c6sc01011c 10.1038/s41401-020-0485-4 10.1021/bi702203w 10.1038/s41594-020-0479-4 10.5582/bst.2020.01047 10.1517/17460441.2015.1032936 10.12932/AP-030520-0826 10.1038/s41586-020-2179-y 10.1021/acs.jpcb.0c04511 10.1038/s41422-021-00495-9 10.3390/v12101164 10.1261/rna.7640104 10.1016/j.softx.2015.06.001 10.1021/acs.jcim.7b00347 10.1136/bmj.m606 10.1021/ct300418h 10.1038/s41586-020-2180-5 10.1007/s12539-021-00462-3 10.3389/fmolb.2017.00087 10.26633/RPSP.2020.40 10.1002/cbic.202000047 10.1126/science.abb2762 10.1007/s11356-021-16250-x 10.1080/17441692.2020.1783340 10.1038/s41586-020-2665-2 10.1016/j.cmi.2020.09.023 10.1093/cid/ciaa601 10.1128/JVI.01281-09 10.1007/s10822-010-9352-6 10.1016/j.meegid.2021.104773 10.1056/NEJMoa2103055 10.1021/ci6002202 10.1002/jmv.26165 10.12659/MSM.928996 10.1038/s41423-020-0458-z 10.1056/NEJMc2104974 10.1056/NEJMoa2108891 10.3390/membranes10090215 10.1007/978-1-4939-7000-1_26 10.3390/pathogens9030231 10.1021/acs.jctc.1c00645 |
ContentType | Journal Article |
Copyright | 2023 Informa UK Limited, trading as Taylor & Francis Group 2023 |
Copyright_xml | – notice: 2023 Informa UK Limited, trading as Taylor & Francis Group 2023 |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 |
DOI | 10.1080/07391102.2023.2274514 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
DatabaseTitleList | MEDLINE MEDLINE - Academic |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1538-0254 |
EndPage | 5868 |
ExternalDocumentID | 37938133 10_1080_07391102_2023_2274514 2274514 |
Genre | Research Article Journal Article |
GroupedDBID | --- -~X .QJ 0BK 0R~ 30N 4.4 5GY AAENE AAHBH AAJMT AALDU AAMIU AAPUL AAQRR ABCCY ABFIM ABJNI ABLIJ ABPAQ ABPEM ABTAI ABXUL ABXYU ACGFS ACTIO ADCVX ADGTB AEISY AENEX AEOZL AEPSL AEYOC AGDLA AGMYJ AHDZW AIJEM AKBVH AKOOK ALMA_UNASSIGNED_HOLDINGS ALQZU AQRUH AVBZW AWYRJ BLEHA CCCUG DGEBU DKSSO EBS E~A E~B F5P GTTXZ H13 HZ~ H~P IPNFZ J.P KYCEM LJTGL M4Z NX0 O9- P2P RIG RNANH ROSJB RTWRZ S-T SJN SNACF TBQAZ TDBHL TEI TFL TFT TFW TQWBC TTHFI TUROJ UT5 ZGOLN ~KM ~S~ AAGDL AAHIA AAYXX ADYSH AFRVT AIYEW AMPGV CITATION EMOBN 07X 53G AAGME AAOAP ABFMO ABTAA ACBBU ACDHJ ACQMU ACZPZ ADGTR ADOPC AFDYB AFFVI AI. AMATQ APNXG AURDB BFWEY C0. CGR CUY CVF CWRZV DLOXE ECM EIF EJD HGUVV JEPSP NPM NUSFT OWHGL PCLFJ S70 TASJS VH1 7X8 |
ID | FETCH-LOGICAL-c314t-99ca9b9c55c2bca49d97b3ce35690e84ceb39d63731fa4f200eaab9ebcc9e9113 |
ISSN | 0739-1102 1538-0254 |
IngestDate | Thu Sep 04 21:22:52 EDT 2025 Mon Jul 21 06:03:35 EDT 2025 Tue Jul 01 00:57:01 EDT 2025 Wed Dec 25 09:05:42 EST 2024 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 11 |
Keywords | peptide inhibitors ACE2 SARS-CoV-2 variants molecular dynamics |
Language | English |
LinkModel | OpenURL |
MergedId | FETCHMERGED-LOGICAL-c314t-99ca9b9c55c2bca49d97b3ce35690e84ceb39d63731fa4f200eaab9ebcc9e9113 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 37938133 |
PQID | 2887476254 |
PQPubID | 23479 |
PageCount | 11 |
ParticipantIDs | crossref_primary_10_1080_07391102_2023_2274514 pubmed_primary_37938133 proquest_miscellaneous_2887476254 informaworld_taylorfrancis_310_1080_07391102_2023_2274514 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2024-07-23 |
PublicationDateYYYYMMDD | 2024-07-23 |
PublicationDate_xml | – month: 07 year: 2024 text: 2024-07-23 day: 23 |
PublicationDecade | 2020 |
PublicationPlace | England |
PublicationPlace_xml | – name: England |
PublicationTitle | Journal of biomolecular structure & dynamics |
PublicationTitleAlternate | J Biomol Struct Dyn |
PublicationYear | 2024 |
Publisher | Taylor & Francis |
Publisher_xml | – name: Taylor & Francis |
References | e_1_3_2_28_1 e_1_3_2_49_1 e_1_3_2_20_1 e_1_3_2_41_1 e_1_3_2_22_1 e_1_3_2_43_1 e_1_3_2_24_1 e_1_3_2_45_1 e_1_3_2_26_1 e_1_3_2_47_1 e_1_3_2_16_1 e_1_3_2_39_1 e_1_3_2_9_1 e_1_3_2_18_1 e_1_3_2_7_1 e_1_3_2_31_1 e_1_3_2_10_1 e_1_3_2_33_1 e_1_3_2_12_1 e_1_3_2_35_1 e_1_3_2_5_1 e_1_3_2_14_1 e_1_3_2_37_1 e_1_3_2_3_1 e_1_3_2_50_1 e_1_3_2_27_1 e_1_3_2_29_1 e_1_3_2_42_1 e_1_3_2_21_1 e_1_3_2_44_1 e_1_3_2_23_1 e_1_3_2_46_1 e_1_3_2_25_1 e_1_3_2_48_1 Sivapalasingam S. (e_1_3_2_40_1) 2022 e_1_3_2_17_1 e_1_3_2_38_1 e_1_3_2_8_1 e_1_3_2_19_1 e_1_3_2_2_1 e_1_3_2_30_1 e_1_3_2_11_1 e_1_3_2_32_1 e_1_3_2_6_1 e_1_3_2_13_1 e_1_3_2_34_1 e_1_3_2_4_1 e_1_3_2_15_1 e_1_3_2_36_1 e_1_3_2_51_1 |
References_xml | – ident: e_1_3_2_44_1 doi: 10.1038/s41421-020-00231-4 – ident: e_1_3_2_27_1 doi: 10.1007/s12539-021-00477-w – ident: e_1_3_2_28_1 doi: 10.1186/s40001-022-00647-6 – ident: e_1_3_2_11_1 doi: 10.1016/j.ajpath.2021.10.019 – ident: e_1_3_2_22_1 doi: 10.1016/j.bbrc.2020.11.021 – ident: e_1_3_2_9_1 doi: 10.1101/2020.03.17.20037432 – ident: e_1_3_2_12_1 doi: 10.1136/bmj.n771 – ident: e_1_3_2_24_1 doi: 10.1021/ci500020m – ident: e_1_3_2_33_1 doi: 10.1039/c6sc01011c – ident: e_1_3_2_19_1 doi: 10.1038/s41401-020-0485-4 – ident: e_1_3_2_13_1 doi: 10.1021/bi702203w – ident: e_1_3_2_18_1 doi: 10.1038/s41594-020-0479-4 – ident: e_1_3_2_15_1 doi: 10.5582/bst.2020.01047 – ident: e_1_3_2_16_1 doi: 10.1517/17460441.2015.1032936 – ident: e_1_3_2_20_1 doi: 10.12932/AP-030520-0826 – ident: e_1_3_2_37_1 doi: 10.1038/s41586-020-2179-y – ident: e_1_3_2_32_1 doi: 10.1021/acs.jpcb.0c04511 – ident: e_1_3_2_51_1 doi: 10.1038/s41422-021-00495-9 – ident: e_1_3_2_30_1 doi: 10.3390/v12101164 – ident: e_1_3_2_39_1 doi: 10.1261/rna.7640104 – ident: e_1_3_2_2_1 doi: 10.1016/j.softx.2015.06.001 – ident: e_1_3_2_4_1 doi: 10.1021/acs.jcim.7b00347 – ident: e_1_3_2_47_1 doi: 10.1136/bmj.m606 – ident: e_1_3_2_29_1 doi: 10.1021/ct300418h – ident: e_1_3_2_25_1 doi: 10.1038/s41586-020-2180-5 – ident: e_1_3_2_26_1 doi: 10.1007/s12539-021-00462-3 – ident: e_1_3_2_43_1 doi: 10.3389/fmolb.2017.00087 – ident: e_1_3_2_35_1 doi: 10.26633/RPSP.2020.40 – ident: e_1_3_2_31_1 doi: 10.1002/cbic.202000047 – year: 2022 ident: e_1_3_2_40_1 article-title: Efficacy and safety of sarilumab in hospitalized patients with COVID-19: A randomized clinical trial publication-title: Clinical Infectious Diseases. – ident: e_1_3_2_48_1 doi: 10.1126/science.abb2762 – ident: e_1_3_2_49_1 doi: 10.1007/s11356-021-16250-x – ident: e_1_3_2_17_1 doi: 10.1080/17441692.2020.1783340 – ident: e_1_3_2_21_1 doi: 10.1038/s41586-020-2665-2 – ident: e_1_3_2_46_1 doi: 10.1016/j.cmi.2020.09.023 – ident: e_1_3_2_14_1 doi: 10.1093/cid/ciaa601 – ident: e_1_3_2_10_1 doi: 10.1128/JVI.01281-09 – ident: e_1_3_2_36_1 doi: 10.1007/s10822-010-9352-6 – ident: e_1_3_2_6_1 doi: 10.1016/j.meegid.2021.104773 – ident: e_1_3_2_38_1 doi: 10.1056/NEJMoa2103055 – ident: e_1_3_2_41_1 doi: 10.1021/ci6002202 – ident: e_1_3_2_23_1 doi: 10.1002/jmv.26165 – ident: e_1_3_2_45_1 doi: 10.12659/MSM.928996 – ident: e_1_3_2_50_1 doi: 10.1038/s41423-020-0458-z – ident: e_1_3_2_3_1 doi: 10.1056/NEJMc2104974 – ident: e_1_3_2_7_1 doi: 10.1056/NEJMoa2108891 – ident: e_1_3_2_5_1 doi: 10.3390/membranes10090215 – ident: e_1_3_2_8_1 doi: 10.1007/978-1-4939-7000-1_26 – ident: e_1_3_2_34_1 doi: 10.3390/pathogens9030231 – ident: e_1_3_2_42_1 doi: 10.1021/acs.jctc.1c00645 |
SSID | ssj0021171 |
Score | 2.373723 |
Snippet | COVID-19 has rapidly proliferated around 180 countries, and new cases are reported frequently. No peptide medication has been developed that can reliably block... |
SourceID | proquest pubmed crossref informaworld |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 5858 |
SubjectTerms | ACE2 Angiotensin-Converting Enzyme 2 - chemistry Angiotensin-Converting Enzyme 2 - metabolism Animals Antimicrobial Peptides - chemistry Antimicrobial Peptides - pharmacology Antiviral Agents - chemistry Antiviral Agents - pharmacology Arthropod Proteins - chemistry Binding Sites COVID-19 - virology COVID-19 Drug Treatment Eosinophil Cationic Protein - chemistry Eosinophil Cationic Protein - metabolism Humans Molecular Docking Simulation molecular dynamics Molecular Dynamics Simulation peptide inhibitors Protein Binding SARS-CoV-2 SARS-CoV-2 - drug effects Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - metabolism variants |
Title | Molecular dynamic simulation reveals spider antimicrobial peptide Latarcin-1 and human eosinophil cationic protein as peptide inhibitors of SARS-CoV-2 variants |
URI | https://www.tandfonline.com/doi/abs/10.1080/07391102.2023.2274514 https://www.ncbi.nlm.nih.gov/pubmed/37938133 https://www.proquest.com/docview/2887476254 |
Volume | 42 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1ba9swFBZZx0Zfxu7rbmiwt-AQW77pMYSNMto-bO3om5FkmQgWOxB3tPszg_3SnSPJl0DKLi8m8UVx_H0-OpLOdw4h76FTz7NSzIMqz1CSU8pAcnivVK4xGKDKMpvU5_QsPb6IP10ml5PJr1HU0lUrZ-rHXl3J_6AK-wBXVMn-A7J9o7ADPgO-sAWEYftXGJ92tW2npSssP92ata_HhaIUjbmRt1gDFiMlW7M2Nu0Siq8wmKXU0xPRYjGhOgjtKoKr2Kebrambzcp8m7oJPWjY5nMwNZal6a419cpIY6v1oPJl8flLsGy-BtH0O4y_hU8RtcfxRcV_f-Mufy2uYiAH_d_o_fylcDO5K-07WJsqeLX2cUILOLkPLj7xknlzbcZTGVGMc6RObTzTg_lFff7YPsfRmIfhyNrCUCff2w34uMmMgSm3cruIzSIYfydOsDqixmZtucHATOUhY0Ov2McqdofukLtRBv4ZyoTmZ_2gPgyzsFOGYc72fb95SO53rey4PzvJcW8f4lhX5_wheeChogtHuEdkouvH5J6rWnrzhPzsaUc9XnSgHfW0o452dId21FOHDrSDE0pqaUcH2tGOdtTTjoptf-1AO9pUdKAd7Wj3lFx8_HC-PA58nY9AsTBuA86V4JKrJFGRVCLmJc8kU5olKZ_rPFZaMl6mLGNhJeIKLIAWQnItleIanjZ7Rg7qptYvCC1FGbO5ytNY6phj54NfhA4rnabgmh-RWff4i41L51KEXZZcD12B0BUeuiPCxyAVrZ1Hq1zRm4L94dp3HaIFGG1ciRO1bq62RQRdewxuSALnPHdQ97fTMeXlrUdekcPh7XlNDuBF1W_ANW7lW8vN3zZUuZw |
linkProvider | Taylor & Francis |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwELZQKwQXypsCBSNx9bKJnYePVUW1wO4eaIt6s_yKapUmqyaLBH-Gv8qMk6zaShWHHqPYTmzPeGbs8fcR8hGMelk4PWVVWeCVHGeYkaBXtvSYDFAVRQT1WSzz2Yn4epqdXrkLg2mVGENXPVBEXKtRuXEzekyJ-4SnS2C28B5VyicpBFYZcllvZ-COY1ofny43QVeSxKALqzCsM97iua2Za_bpGnrp7T5otEWHO8SOvehTUM4n685M7J8bAI936-Zj8mhwVel-L1tPyD1fPyX3e_LK38_I38XIrEtdT2tP23AxsIFRRIYCyaYtMtBeUpi_cBEi6BM0ucJUGufpXHdIZVSzBAo4GvkCqW_aUDers_CT9tuJ0HBEkwg11e2mbqjPggnIFUSbih7tfz9iB80PltJfEP1jcs9zcnL4-fhgxga6B2Z5IjompdXSSJtlNjVWC-lkYbj1PIMI3pfCQtwvXc4LnlRaVKDeXmsjvbFWehgo_oJs1U3tXxHqtBN8astcGC8krkH4oH1S-TwHD22XTMZJVqse1UMlI1jqMOoKR10No75L5FVRUF3cTql67hPF_1P3wyg3CnQXD2R07Zt1q1JY4QVYowzKvOwFavM7HH66TDh_fYcvvycPZseLuZp_WX57Qx7CK4Hb0il_S7a6y7XfA3-qM--iwvwDtTgUGQ |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Lb9QwELZQEYhLeUN5Gomrl03sPHysCqsC7QpRirhZfkW1oMmqyVaCP8NfZcZOVhSp4tBjFI8T2zMejz3-PkJeg1OvK6fnrKkrvJLjDDMS7MrWHpMBmqqKoD6Hy3L_WHz4VkzZhP2YVokxdJOAIuJcjca9cs2UEfcGD5fAa-E1qpzPcoirCqSyvl7OuUT4fD5fbmKuLIsxF4owlJku8VxWzQX3dAG89PIlaHRFi9vETI1IGSjfZ-vBzOyvf_Adr9TKO2R7XKjS3aRZd8k1394jNxJ15c_75PfhxKtLXSK1p304HbnAKOJCgV7THvlnzyiMXjgNEfIJqlxhIo3z9EAPSGTUsgwKOBrZAqnv-tB2q5Pwg6bNRKg4YkmElup-Ixvak2ACMgXRrqFHu5-P2F73leX0HGJ_TO15QI4X777s7bOR7IFZnomBSWm1NNIWhc2N1UI6WRluPS8gfve1sBD1S1fyimeNFg0Yt9faSG-slR46ij8kW23X-seEOu0En9u6FMYLiTMQPmifNb4sYX22Q2bTGKtVwvRQ2QSVOva6wl5XY6_vEPm3JqghbqY0iflE8f_IvprURoHl4nGMbn237lUO87sAX1RAmUdJnza_w-Gn64zzJ1f48kty89PbhTp4v_z4lNyCNwL3pHP-jGwNZ2v_HBZTg3kRzeUPXDASxg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Molecular+dynamic+simulation+reveals+spider+antimicrobial+peptide+Latarcin-1+and+human+eosinophil+cationic+protein+as+peptide+inhibitors+of+SARS-CoV-2+variants&rft.jtitle=Journal+of+biomolecular+structure+%26+dynamics&rft.au=Cao%2C+Cheng&rft.au=Mehmood%2C+Aamir&rft.au=Li%2C+Daixi&rft.date=2024-07-23&rft.eissn=1538-0254&rft.volume=42&rft.issue=11&rft.spage=5858&rft_id=info:doi/10.1080%2F07391102.2023.2274514&rft_id=info%3Apmid%2F37938133&rft.externalDocID=37938133 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0739-1102&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0739-1102&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0739-1102&client=summon |