Do Rhodium(III) Complexes Behave as Biocompatible Materials for α-Chymotrypsin Structural Stability and Activity?

In this research study, a series of four acyl thiourea ligands and their corresponding rhodium(III) pentamethylcyclopentadienyl complexes, designated as Rh1, Rh2, Rh3, and Rh4, were successfully used to explore their suitability for a biological macromolecule, i.e., α-chymotrypsin (α-CT). Through meticulous analysis of the spectroscopic data, it was convincingly established that the acyl thiourea ligands served as neutral and monodentate ligands in their interaction with the Rh(III) ions. Specifically, the spectroscopic evidence confirmed that the sulfur (S) atoms within the acyl thiourea ligands formed coordinated bonds with the Rh(III) ions. This crucial finding elucidates the specific coordination mode and binding interactions between the ligands and the central Rh(III) metal ion, which have seldom been investigated. Importantly, various biophysical studies and enzymatic activity results suggested that the structural stability of α-CT was maintained in these Rh(III) complexes. Interestingly, the metal complexes enhanced the thermal stability of α-CT, as indicated by an increase in the transition temperature (<i>T</i><sub>m</sub>) of α-CT. This study unveils the promising role of Rh(III) metal complexes in the stabilization and activation of the biological macromolecule, which further holds potential in industrial and biomedical applications.

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Publication Details

Journal
ACS Applied Bio Materials
Published
2025-11-11
DOI
https://doi.org/10.1021/acsabm.5c01949
Citations
1
Primary Topic
Metal complexes synthesis and properties
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article
Field-Weighted Citation Impact
1.05
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article

Do Rhodium(III) Complexes Behave as Biocompatible Materials for α-Chymotrypsin Structural Stability and Activity?

Pannuru Venkatesu, Jayachandra Prakasan Jayadharini, Deepak Chahar, Pooja Yadav et al.
1 citations
ACS Applied Bio Materials
Metal complexes synthesis and properties
1.05
article

Do Rhodium(III) Complexes Behave as Biocompatible Materials for α-Chymotrypsin Structural Stability and Activity?

Pannuru Venkatesu, Jayachandra Prakasan Jayadharini, Deepak Chahar, Pooja Yadav, Jebiti Haribabu, Ramasamy Karvembu, Anamika Sindhu
article en
1 citations

Abstract

In this research study, a series of four acyl thiourea ligands and their corresponding rhodium(III) pentamethylcyclopentadienyl complexes, designated as Rh1, Rh2, Rh3, and Rh4, were successfully used to explore their suitability for a biological macromolecule, i.e., α-chymotrypsin (α-CT). Through meticulous analysis of the spectroscopic data, it was convincingly established that the acyl thiourea ligands served as neutral and monodentate ligands in their interaction with the Rh(III) ions. Specifically, the spectroscopic evidence confirmed that the sulfur (S) atoms within the acyl thiourea ligands formed coordinated bonds with the Rh(III) ions. This crucial finding elucidates the specific coordination mode and binding interactions between the ligands and the central Rh(III) metal ion, which have seldom been investigated. Importantly, various biophysical studies and enzymatic activity results suggested that the structural stability of α-CT was maintained in these Rh(III) complexes. Interestingly, the metal complexes enhanced the thermal stability of α-CT, as indicated by an increase in the transition temperature (<i>T</i><sub>m</sub>) of α-CT. This study unveils the promising role of Rh(III) metal complexes in the stabilization and activation of the biological macromolecule, which further holds potential in industrial and biomedical applications.

ACS Applied Bio MaterialsVol. 8(12)
University of Delhi (IN), National Institute of Technology Tiruchirappalli (IN), University of Atacama (CL)
Openalex Percentile: Top 16%
Metal complexes synthesis and properties
1.05
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Do Rhodium(III) Complexes Behave as Biocompatible Materials for α-Chymotrypsin Structural Stability and Activity? — Pannuru Venkatesu, Jayachandra Prakasan Jayadharini, et al. · ACS Applied Bio Materials (2025) | TGRS Research Map | TGRS