Evidence map›Paper›PMID 39318003›Full record

ArticleCurrent medicinal chemistry2026

Morpholine-tethered Novel Hydrazones as Promising Non-peptidic Prolyl Oligopeptidase (POP) Inhibitors: Synthesis

Urwa Khalid, Noor Fatima, Saeed Ullah, Sobia Ahsan Halim, Ajmal Khan, Suraj N Mali, Attalla F El-Kott, Mohammed A AlShehri, Hamdy Kashtoh, Ahmed Al-Harrasi and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Current medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Urwa KhalidInstitute of Chemical Sciences, Bahauddin Zakariya University, Multan, 60800, Pakistan.
Noor FatimaInstitute of Chemical Sciences, Bahauddin Zakariya University, Multan, 60800, Pakistan.
Saeed UllahNatural and Medical Sciences Research Centre, University of Nizwa, P.O. Box 33, PC 616, Birkat Al Mauz, Nizwa, Sultanate of Oman.
Sobia Ahsan HalimNatural and Medical Sciences Research Centre, University of Nizwa, P.O. Box 33, PC 616, Birkat Al Mauz, Nizwa, Sultanate of Oman.
Ajmal KhanNatural and Medical Sciences Research Centre, University of Nizwa, P.O. Box 33, PC 616, Birkat Al Mauz, Nizwa, Sultanate of Oman.
Suraj N MaliDepartment of Pharmaceutical Science and Technology, Birla Institute of Technology, Mesra, 835215, India.
Attalla F El-KottDepartment of Biology, College of Science, King Khalid University, Abha, Saudi Arabia.
Mohammed A AlShehriDepartment of Biology, College of Science, King Khalid University, Abha, Saudi Arabia.
Hamdy KashtohDepartment of Biotechnology, Yeungnam University, Gyeongsan, 38541, Gyeongbuk, Republic of Korea.
Ahmed Al-HarrasiNatural and Medical Sciences Research Centre, University of Nizwa, P.O. Box 33, PC 616, Birkat Al Mauz, Nizwa, Sultanate of Oman.
Zahid ShafiqInstitute of Chemical Sciences, Bahauddin Zakariya University, Multan, 60800, Pakistan.

Funding

Deanship of Scientific Research at King Khalid University RGP1/15/45
6 · The paper itself

Abstract

introductionProlyl oligopeptidase (POP) is a pivotal druggable target implicated in diverse biological processes and linked to the development of various ailments, including neurodegenerative disorders. While conventional peptide-based inhibitors have been a centerpiece, their limitations, such as restricted bioavailability, necessitate exploration of non-peptidic inhibitors for their therapeutic potential.

methodsThis study focuses on designing, synthesizing, and assessing morpholine- based hydrazones targeting the catalytic serine residue of POP. The hydrazones (5a-o), reported as moderately potent analogs compared to the renowned Z-Pro-Prolinal, demonstrated in vitro POP inhibition with IC

resultsMoreover, the in vitro kinetic study of compound 5h indicated that it exhibited concentration-dependent type of inhibition. In silico docking studies of 5h revealed robust interactions in the POP enzyme's active site, yielding a docking score of -6.30 Kcal/- mol, consistent with experimental results.

conclusionAll findings underscored the potential of synthesized derivatives for drug development.

Indexed as

HydrazonesMorpholinesSerine EndopeptidasesSerine Proteinase InhibitorsHumansMolecular Docking SimulationMolecular StructureProlyl OligopeptidasesStructure-Activity RelationshipHydrazonesmorpholineMorpholinesPREPL protein, humanProlyl OligopeptidasesSerine EndopeptidasesSerine Proteinase Inhibitorsantimicrobial.hydrazonesmolecular dockingmorpholineprolyl endopeptidase (PEP)Prolyl oligopeptidase (POP)

Identifiers

PMID39318003

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.