Evidence map›Paper›PMID 41952598›Full record

ArticleACS applied materials & interfaces2026

Site-Specific Abiraterone Protein-Drug Conjugates via Hedgehog Autoprocessing.

Asma Gulzar, Laiba Maryam, Sisila Valappil, Vivanthi Thanthrige, Ebbing de Jong, Miguel Guzman, Md Shahadat Hossain, Atanu Acharya, Davoud Mozhdehi

Abstract read
In one paragraph

Article in ACS applied materials & interfaces, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

9 authors.

Asma GulzarDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0009-0004-8978-5648
Laiba MaryamDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0009-0001-5941-1870
Sisila ValappilDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0000-0002-5544-3226
Vivanthi ThanthrigeDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Ebbing de JongUpstate Medical University, Proteomics and Mass Spectrometry, Weiskotten Hall 4307 WHA, 766 Irving Avenue, Syracuse, New York 13210, United States.
Miguel GuzmanDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Md Shahadat HossainDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.
Atanu AcharyaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0000-0002-6960-7789
Davoud MozhdehiDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, New York 13244, United States.ORCID 0000-0002-3440-8878

Funding

Investigation of Long-Range Charge Transfer and Excited State Processes in Biochemical SystemsR35GM150874 · NIGMS · SYRACUSE UNIVERSITY · PI Atanu Acharya · 2023 to 2026
$1.5M
NIGMS NIH HHS R35 GM150874
6 · The paper itself

Abstract

Protein lipoengineering is a promising approach for programming biomolecular assembly and function, yet its use has remained confined to biologically inert lipids. Here, we repurpose the hedgehog autoprocessing domain as a biocatalyst to install the anticancer sterol abiraterone as a noncanonical post-translational modification (ncPTM) on an intrinsically disordered protein scaffold. Artificial abirateronylation produced protein-drug conjugates (PDCs) with significantly enhanced solubility, tunable phase behavior, and dynamic self-association. The conjugates underwent slow hydrolytic release of abiraterone and reproduced the cytotoxic response of the free drug in prostate-cancer cells, achieving more uniform activity and distributions in 3D tumor spheroids. By extending this approach to a second steroidal prostate-cancer agent, galeterone, we demonstrate a generalizable ncPTM strategy for exploiting native lipidation machinery to construct molecularly defined, programmable protein-drug therapeutics.

Indexed as

AndrostenesHedgehog ProteinsProtein Processing, Post-TranslationalAntineoplastic AgentsBiocatalysisCell Line, TumorCell SurvivalHumansMolecular Docking SimulationProstatic NeoplasmsProtein Structure, TertiarySubstrate SpecificityabirateroneAndrostenesAntineoplastic AgentsHedgehog Proteinsabirateronehedgehoglipoengineeringpost-translational modificationprotein–drug conjugate, prostate cancer

Identifiers

PMID41952598
PMCPMC13107367

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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.