---
title: "Masked Bisphosphonate Inhibitors of Acid Sphingomyelinase: Enhanced Cell Penetration and Potency"
id: "pubmed-42842989"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42842989"
content_type: "clinical_feed_article"
specialty: "Critical Care"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42842989/"
doi: "10.1021/acschembio.6c00541"
published_at: "2026-10-08T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Masked Bisphosphonate Inhibitors of Acid Sphingomyelinase: Enhanced Cell Penetration and Potency
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42842989
- **Specialty:** [Critical Care](https://medichelpline.com/clinical-feed/critical-care.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42842989/)
- **DOI:** [10.1021/acschembio.6c00541](https://doi.org/10.1021%2Facschembio.6c00541)
- **Published At:** 2026-10-08T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- The study reports development of masked **bisphosphonate** derivatives of the amino bisphosphonate inhibitor **ARC39** that inhibit **acid sphingomyelinase (ASM)** with **nanomolar** in cellulo activity. - Masking of ARC39 produced derivatives that are approximately **100 times** more potent in cell-based assays than the parent compound. - **ASM** catalyzes conversion of sphingomyelin to ceramide, a lipid mediator implicated in cancer, metastasis, acute lung injury, sepsis, atherosclerosis, and major depression; ASM is therefore a target of therapeutic interest. - The authors thoroughly evaluated properties relevant to cellular pharmacology, including **cell uptake** and **stability** of the masked derivatives; specific experimental details and quantitative results beyond potency were not reported in the PubMed abstract. - The work addresses an unmet need for potent ASM inhibitors and suggests that masking bisphosphonate functionality can improve cellular delivery and functional potency. - The study was published in ACS Chemical Biology and supported by Deutsche Forschungsgemeinschaft grants listed in the article metadata. - Exact experimental methods, full potency values, structure–activity relationships, in vivo data, and safety/toxicity findings were not provided in the source abstract and are not inferred here.
## Clinical Analysis & Structured Key Points
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Online ahead of print. # Masked Bisphosphonate Inhibitors of Acid Sphingomyelinase: Improved Cell Penetration and Potency [Christian Kappe](https://pubmed.ncbi.nlm.nih.gov/?term=Kappe+C&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany."), [Marcel Rühling](https://pubmed.ncbi.nlm.nih.gov/?term=R%C3%BChling+M&cauthor_id=42842989)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-2 "Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany."), [Rama Machlah](https://pubmed.ncbi.nlm.nih.gov/?term=Machlah+R&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Fabian Schumacher](https://pubmed.ncbi.nlm.nih.gov/?term=Schumacher+F&cauthor_id=42842989)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-4 "Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany."), [Maria Russi](https://pubmed.ncbi.nlm.nih.gov/?term=Russi+M&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany."), [Eyad Naser](https://pubmed.ncbi.nlm.nih.gov/?term=Naser+E&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Alexander Carpinteiro](https://pubmed.ncbi.nlm.nih.gov/?term=Carpinteiro+A&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Burkhard Kleuser](https://pubmed.ncbi.nlm.nih.gov/?term=Kleuser+B&cauthor_id=42842989)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-4 "Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany."), [Martin Fraunholz](https://pubmed.ncbi.nlm.nih.gov/?term=Fraunholz+M&cauthor_id=42842989)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-2 "Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany."), [Christoph Arenz](https://pubmed.ncbi.nlm.nih.gov/?term=Arenz+C&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#full-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany.") Affiliations Expand ### Affiliations * 1 Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany. * 2 Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany. * 3 Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany. * 4 Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany. * PMID: **42842989** * DOI: [ 10.1021/acschembio.6c00541 ](https://doi.org/10.1021/acschembio.6c00541) Item in Clipboard # Masked Bisphosphonate Inhibitors of Acid Sphingomyelinase: Improved Cell Penetration and Potency Christian Kappe et al. ACS Chem Biol. 2026. Show details Display options Display options Format Abstract PubMed PMID ACS Chem Biol Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22ACS+Chem+Biol%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22ACS+Chem+Biol%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42842989/) . 2026 Oct 8. doi: 10.1021/acschembio.6c00541. Online ahead of print. ### Authors [Christian Kappe](https://pubmed.ncbi.nlm.nih.gov/?term=Kappe+C&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany."), [Marcel Rühling](https://pubmed.ncbi.nlm.nih.gov/?term=R%C3%BChling+M&cauthor_id=42842989)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-2 "Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany."), [Rama Machlah](https://pubmed.ncbi.nlm.nih.gov/?term=Machlah+R&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Fabian Schumacher](https://pubmed.ncbi.nlm.nih.gov/?term=Schumacher+F&cauthor_id=42842989)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-4 "Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany."), [Maria Russi](https://pubmed.ncbi.nlm.nih.gov/?term=Russi+M&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany."), [Eyad Naser](https://pubmed.ncbi.nlm.nih.gov/?term=Naser+E&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Alexander Carpinteiro](https://pubmed.ncbi.nlm.nih.gov/?term=Carpinteiro+A&cauthor_id=42842989)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-3 "Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany."), [Burkhard Kleuser](https://pubmed.ncbi.nlm.nih.gov/?term=Kleuser+B&cauthor_id=42842989)[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-4 "Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany."), [Martin Fraunholz](https://pubmed.ncbi.nlm.nih.gov/?term=Fraunholz+M&cauthor_id=42842989)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-2 "Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany."), [Christoph Arenz](https://pubmed.ncbi.nlm.nih.gov/?term=Arenz+C&cauthor_id=42842989)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42842989/#short-view-affiliation-1 "Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany.") ### Affiliations * 1 Institut für Chemie, Humboldt Universität zu Berlin, Brook-Taylor-Str 2, 12489Berlin, Germany. * 2 Chair of Microbiology, Julius-Maximilians-University Würzburg, 97074Würzburg, Germany. * 3 Institute of Molecular Biology, University of Duisburg-Essen, 45147Essen, Germany. * 4 Institute of Pharmacy, Freie Universität Berlin, Königin-Luise-Str. 2+4, 14195Berlin, Germany. * PMID: **42842989** * DOI: [ 10.1021/acschembio.6c00541 ](https://doi.org/10.1021/acschembio.6c00541) Item in Clipboard Cite Display options Display options Format Abstract PubMed PMID Linked Discoveries ## Abstract Inhibitors of acid sphingomyelinase (ASM) with nanomolar in cellulo activity were developed by masking the amino bisphosphonate inhibitor ARC39. ASM is a key enzyme catalyzing the hydrolysis of sphingomyelin to ceramide, which plays a role in various physiological and pathological processes. Inhibitors of ASM have been proposed as potential treatment for disorders such as cancer and metastasis, acute lung injury, sepsis, atherosclerosis, and major depression. Despite the vital interest in ASM as a drug target, potent inhibitors of this enzyme are still urgently needed. The masked ARC39 derivatives developed in this study are 100 times more potent than the parent compound. Their properties such as cell uptake, stability, etc. were thoroughly investigated. © 2026 The Authors. Published by American Chemical Society. 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