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Record W4246069255 · doi:10.26434/chemrxiv.13288463

Covalent and Non-Covalent Binding Free Energy Calculations for Peptidomimetic Inhibitors of SARS-CoV-2 Main Protease

2020· preprint· en· W4246069255 on OpenAlexaff
Ernest Awoonor‐Williams, Abd Al‐Aziz A. Abu‐Saleh

Bibliographic record

VenueChemRxiv · 2020
Typepreprint
Languageen
FieldComputer Science
TopicComputational Drug Discovery Methods
Canadian institutionsMemorial University of Newfoundland
Fundersnot available
KeywordsPeptidomimeticCovalent bondChemistryStereochemistryProteaseBinding siteCoronavirus disease 2019 (COVID-19)Ligand (biochemistry)Binding energySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Combinatorial chemistryVirologyEnzymeBiochemistryMedicineReceptorInfectious disease (medical specialty)PhysicsOrganic chemistry

Abstract

fetched live from OpenAlex

COVID-19, the disease caused by the newly discovered coronavirus — SARS-CoV-2, has created global health, social, and economic crisis. At the time of writing (November 12, 2020), there are over 50 million confirmed cases and more than 1 million reported deaths due to COVID-19. Currently, there are no approved vaccines, and recently Veklury (remdesivir) was approved for the treatment of COVID-19 requiring hospitalization. The main protease (M<sup>pro</sup>) of the virus is an attractive target for the development of effective antiviral therapeutics because it is required for proteolytic cleavage of viral polyproteins. Furthermore, the M<sup>pro</sup> has no human homologues, so drugs designed to bind to this target directly have less risk for off-target reactivity. Recently, several high-resolution crystallographic structures of the M<sup>pro</sup> in complex with inhibitors have been determined — to guide drug development and to spur efforts in structure-based drug design. One of the primary objectives of modern structure-based drug design is the accurate prediction of receptor­-ligand binding affinities for rational drug design and discovery. Here, we perform rigorous alchemical absolute binding free energy calculations and QM/MM calculations to give insight into the total binding energy of two recently crystallized inhibitors of SARS-CoV-2 M<sup>pro</sup>, namely, N3 and α-ketoamide 13b. The total binding energy consists of both covalent and non-covalent binding components since both compounds are covalent inhibitors of the M<sup>pro</sup>. Our results indicate that the covalent and non-covalent binding free energy contributions of both inhibitors to the M<sup>pro</sup> target differ significantly. The N3 inhibitor has more favourable non-covalent interactions, particularly hydrogen bonding, in the binding site of the M<sup>pro</sup> than the α-ketoamide inhibitor. But the Gibbs energy of reaction for the M<sup>pro</sup>–α-ketoamide covalent adduct is greater than the Gibbs reaction energy for the M<sup>pro</sup>–N3 covalent adduct. These differences in the covalent and non-covalent binding free energy contributions for both inhibitors could be a plausible explanation for their in vitro differences in antiviral activity. Our findings highlight the importance of both covalent and non-covalent binding free energy contributions to the absolute binding affinity of a covalent inhibitor towards its target.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.001
metaresearch head score (Gemma)0.001
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesMeta-epidemiology (narrow)
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: none
GenreCandidate signal: Methods · Consensus signal: none
Teacher disagreement score0.425
Threshold uncertainty score1.000

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0010.001
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0010.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0010.003
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.060
GPT teacher head0.323
Teacher spread0.263 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

Study designBench or experimental
Domainnot available
GenreMethods

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations4
Published2020
Admission routes1
Has abstractyes

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