kth.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Discovery of Cell-Permeable Allosteric Inhibitors of Liver Pyruvate Kinase: Design and Synthesis of Sulfone-Based Urolithins
Trustlife Labs Drug Research & Development Center, 34774 Istanbul, Türkiye;.
Trustlife Labs Drug Research & Development Center, 34774 Istanbul, Türkiye;.
Trustlife Labs Drug Research & Development Center, 34774 Istanbul, Türkiye;.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Systems Biology. KTH, Centres, Science for Life Laboratory, SciLifeLab.
Show others and affiliations
2024 (English)In: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 25, no 14, article id 7986Article in journal (Refereed) Published
Abstract [en]

Metabolic dysfunction-associated fatty liver disease (MAFLD) presents a significant global health challenge, characterized by the accumulation of liver fat and impacting a considerable portion of the worldwide population. Despite its widespread occurrence, effective treatments for MAFLD are limited. The liver-specific isoform of pyruvate kinase (PKL) has been identified as a promising target for developing MAFLD therapies. Urolithin C, an allosteric inhibitor of PKL, has shown potential in preliminary studies. Expanding upon this groundwork, our study delved into delineating the structure-activity relationship of urolithin C via the synthesis of sulfone-based urolithin analogs. Our results highlight that incorporating a sulfone moiety leads to substantial PKL inhibition, with additional catechol moieties further enhancing this effect. Despite modest improvements in liver cell lines, there was a significant increase in inhibition observed in HepG2 cell lysates. Specifically, compounds 15d, 9d, 15e, 18a, 12d, and 15a displayed promising IC50 values ranging from 4.3 µM to 18.7 µM. Notably, compound 15e not only demonstrated a decrease in PKL activity and triacylglycerol (TAG) content but also showed efficient cellular uptake. These findings position compound 15e as a promising candidate for pharmacological MAFLD treatment, warranting further research and studies.

Place, publisher, year, edition, pages
MDPI AG , 2024. Vol. 25, no 14, article id 7986
Keywords [en]
allosteric PKL inhibition, cell permeability, MAFLD, pyruvate kinase liver, sulfone-based urolithin analogues, TAG content
National Category
Biochemistry Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-351706DOI: 10.3390/ijms25147986ISI: 001277675400001PubMedID: 39063228Scopus ID: 2-s2.0-85199777848OAI: oai:DiVA.org:kth-351706DiVA, id: diva2:1888669
Note

QC 20240814

Available from: 2024-08-13 Created: 2024-08-13 Last updated: 2025-02-20Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records

Kim, WoongheeZhang, ChengUhlén, MathiasMardinoglu, Adil

Search in DiVA

By author/editor
Kim, WoongheeZhang, ChengUhlén, MathiasMardinoglu, Adil
By organisation
Systems BiologyScience for Life Laboratory, SciLifeLabAlbanova VinnExcellence Center for Protein Technology, ProNova
In the same journal
International Journal of Molecular Sciences
BiochemistryMolecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 39 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf