AB028. Selected 10-atom derivatives of mercaptoborate as substrates for the coupling reaction with the neurotransmitter protein
Abstract

AB028. Selected 10-atom derivatives of mercaptoborate as substrates for the coupling reaction with the neurotransmitter protein

Karolina Wójciuk, Michał Dorosz, Rafał Prokopowicz

Nuclear Facilities Operations Department, Reactor Research Division, National Centre for Nuclear Research, Otwock, Poland

Correspondence to: Karolina Wójciuk, PhD. Nuclear Facilities Operations Department, Reactor Research Division, National Centre for Nuclear Research, Andrzeja Soltana 7, 05-400 Otwock, Poland. Email: karolina.wojciuk@ncbj.gov.pl

Background: Cancer remains a major global health challenge in the 21st century. Effective therapy depends on early detection and selective targeting of tumor cells. Boron neutron capture therapy (BNCT), which exploits the selective accumulation of boron-10 followed by neutron irradiation, represents a promising therapeutic approach. Although somatostatin analogs such as octreotide have been clinically applied, novel boron carriers are required. Sauvagine, a peptide ligand for the corticotropin-releasing factor receptor subtype 2a (CRF2a), is relevant because this receptor is expressed in pituitary, pancreatic, central nervous system, prostate, breast, and colorectal tumors. This study aimed to evaluate a new boron-10 cluster carrier based on sauvagine analogs.

Methods: Two compounds—trimethylammonium 1-mercapto-1-carbadodecaborate (TMA) and mercaptododecaborate dianion (BSH)—were tested in colon cancer (HCT116) and normal colon (CCD841) cells. Biochemical and biological properties, including serum stability, lipophilicity, cytotoxicity, half-maximal inhibitory concentration (IC50), and apoptosis induction, were assessed using triplex assays.

Results: TMA, structurally related to clinically applied BSH, showed greater potential as a boron carrier. Its sulfhydryl group enables conjugation with proteins, while the aliphatic chain increases lipophilicity and facilitates blood-brain barrier penetration. TMA localized to membranes within four hours and activated apoptotic pathways in a concentration-dependent manner. At 2 μg/mL, TMA displayed higher cytotoxicity toward cancer cells than BSH. Apoptosis was triggered at nanomolar concentrations, with an increase in late apoptotic populations.

Conclusions: TMA demonstrates favorable biochemical and cytotoxic properties, supporting its potential as a novel boron-10 carrier for BNCT.

Keywords: Boron neutron capture therapy (BNCT); coupling reaction; boron clusters; biological response

Acknowledgments

The authors would like to thank the Institute of Nuclear Chemistry and Technology in Warsaw for the HPLC and ICPMS measurements.

Footnote

Funding: This project was supported by the National Science Centre, Poland (No. 2018/02/X/NZ7/03011).

Conflicts of Interest: All authors have completed the ICMJE uniform disclosure form (available at https://tro.amegroups.com/article/view/10.21037/tro-25-ab028/coif). The authors have no conflicts of interest to declare.

Ethical Statement: The authors are accountable for all aspects of the work in ensuring that questions related to the accuracy or integrity of any part of the work are appropriately investigated and resolved. Ethics approval was not requested for this study as it did not involve laboratory animals or patients.

Open Access Statement: This is an Open Access article distributed in accordance with the Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License (CC BY-NC-ND 4.0), which permits the noncommercial replication and distribution of the article with the strict proviso that no changes or edits are made and the original work is properly cited (including links to both the formal publication through the relevant DOI and the license). See: https://creativecommons.org/licenses/by-nc-nd/4.0/.

doi: 10.21037/tro-25-ab028
Cite this abstract as: Wójciuk K, Dorosz M, Prokopowicz R. AB028. Selected 10-atom derivatives of mercaptoborate as substrates for the coupling reaction with the neurotransmitter protein. Ther Radiol Oncol 2025;9:AB028.

Article Options

Download Citation

Share