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Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
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Structural determinants underlying the supramolecular binding between carborane and proteins in water.

Tainah Dorina Marforio1, Andrea Carboni2, Luca Mazzei3

  • 1Dipartimento di Chimica 'Giacomo Ciamician', Alma Mater Studiorum - Università di Bologna, Via Gobetti 85, 40129 Bologna, Italy; IRCCS Azienda Ospedaliero - Universitaria di Bologna, Preclinical & Translational Research in Oncology Lab (PRO), Bologna, Italy.

Journal of Colloid and Interface Science
|January 10, 2026
PubMed
Summary

Carboranes form stable complexes with proteins like lysozyme, with binding driven by hydrophobic interactions. This discovery aids in developing new carborane-based nanomedicine delivery platforms.

Keywords:
Boron neutron capture therapyCarborane-protein interactionsHydrophobic interactionsMolecular dynamics simulationsSupramolecular binding

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Area of Science:

  • Medicinal Chemistry
  • Nanomedicine
  • Supramolecular Chemistry

Background:

  • Carboranes are stable boron-carbon clusters with potential in medicinal chemistry.
  • Research is shifting towards understanding carborane interactions with biological macromolecules, especially proteins.

Purpose of the Study:

  • To characterize the interaction between closo-ortho-carborane and lysozyme (LSZ).
  • To investigate the binding principles and effects on protein function.
  • To explore the generalizability of carborane-protein interactions.

Main Methods:

  • NMR spectroscopy
  • Molecular docking
  • Molecular dynamics simulations
  • Enzymatic assays

Main Results:

  • Carborane forms a stable 1:1 complex (Carborane@LSZ) with lysozyme, maintaining protein structure.
  • Binding occurs near the substrate-binding pocket, driven by hydrophobic and hydrogen bonding.
  • The Carborane@LSZ complex shows partial inhibition of enzymatic activity (~33%).
  • Similar binding principles were observed with bovine serum albumin (BSA).

Conclusions:

  • Carboranes exhibit specific recognition by proteins through hydrophobic pockets.
  • These interactions are generalizable across different proteins.
  • Findings support the design of carborane-based therapeutics and nanomedicine delivery systems.