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Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS₃ Coordination Environment Imitating Metalloid Binding Sites in Proteins.

ABSTRACT: The As^III binding of two NTA-based tripodal pseudopeptides, possessing three cysteine (ligand L¹) or d-penicillamine residues (ligand L²) as potential coordinating groups for soft semimetals or metal ions, was studied by experimental (UV, CD, NMR, and ESI-MS) and theoretical (DFT) methods. All of the experimental data, obtained with the variation of the As^III:ligand concentration ratios or pH values in some instances, evidence the exclusive formation of species with an AsS₃-type coordination mode. The UV-monitored titration of the ligands with arsenous acid at pH = 7.0 provided an absorbance data set that allowed for the determination of apparent stability constants of the forming species. The obtained stabilities (log

SUBMITTER: Szekeres LI

PROVIDER: S-EPMC10155180 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS₃ Coordination Environment Imitating Metalloid Binding Sites in Proteins.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS3 Coordination Environment Imitating Metalloid Binding Sites in Proteins.

OmicsDI is part of the ELIXIR infrastructure

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Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS₃ Coordination Environment Imitating Metalloid Binding Sites in Proteins.