Evidence map›Paper›PMID 41089481›Full record

ArticleACS medicinal chemistry letters2025

Structure-Guided Temporin L Analogs Development to Inhibit the Main Protease of SARS-CoV‑2.

James Stewart, Ruoqing Jia, Md Ackas Ali, Blaise Williams, Kaylee Stone, Ryan Faddis, Md Shahadat Hossain, Andrew C McShan, Mohammed Akhter Hossain, Mohammad A Halim

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS medicinal chemistry letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

James StewartDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.
Ruoqing JiaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Md Ackas AliDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.
Blaise WilliamsDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.
Kaylee StoneDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.
Ryan FaddisDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.
Md Shahadat HossainDivision of Infectious Diseases and Division of Computer-Aided Drug Design, The Red-Green Research Centre, BICCB, Tejgaon, Dhaka 1215, Bangladesh.ORCID https://orcid.org/0000-0002-6534-3640
Andrew C McShanSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.ORCID https://orcid.org/0000-0002-3212-9867
Mohammed Akhter HossainThe Florey, University of Melbourne, Melbourne, Victoria 3010, Australia.ORCID https://orcid.org/0000-0002-9961-0006
Mohammad A HalimDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, Georgia 30144, United States.ORCID https://orcid.org/0000-0002-1698-7044

Funding

Peach State Bridges to the DoctorateT32GM150548 · NIGMS · KENNESAW STATE UNIVERSITY · PI Kelly A Dyer, Melanie Christine Griffin · 2023 to 2026
$1.3M
NIGMS NIH HHS T32 GM150548
6 · The paper itself

Abstract

Peptide-based inhibitors exhibit considerable potential as antiviral agents targeting SARS-CoV-2. In this study, we designed analogs (TLP-1, TLP-2, and TLP-3) of Temporin L (TL) peptide with the specific objective of selectively interacting with and targeting the main protease (Mpro) of SARS-CoV-2. The synthesis and characterization of TLPs were employed using solid-phase peptide synthesis and LC-MS respectively. CD and solution NMR spectroscopy elucidated the overall structure of the TLPs relative to TL, revealing folded peptides where introduced mutations alter the peptide conformation for binding to Mpro. MD simulations highlighted improvements in TLP's stability and interactions with Mpro. FRET based protease activity assays provided evidence that TLPs exhibited enhanced inhibitory activity against Mpro. The results of our study reveal the promising prospects of TLPs as attractive candidates for

Indexed as

Main ProteaseMolecular DynamicsPeptide inhibitorSARS-CoV-2Temporin L

Identifiers

PMID41089481
PMCPMC12516397

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.