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Updated: May 2, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Disulfide bond cleavage induced by a platinum(II) methionine complex
Haiying Wei1, Xiaoyong Wang, Qin Liu
1State Key Laboratory of Coordination Chemistry, Coordination Chemistry Institute, Nanjing University, 210093 Nanjing, PR China.
A platinum(II) complex, [Pt(Met)Cl2], effectively cleaves disulfide bonds in oxidized glutathione (GSSG). This reaction is significantly faster than with cisplatin, offering insights into platinum complexes within cellular redox systems.
Area of Science:
- Biochemistry
- Inorganic Chemistry
- Chemical Biology
Background:
- Disulfide bond cleavage is crucial for cellular redox balance, involving glutathione (GSH)/oxidized glutathione (GSSG) systems.
- Platinum complexes are used in cancer therapy and can interact with biological thiols and disulfides.
Purpose of the Study:
- To investigate the ability of a platinum(II) complex, [Pt(Met)Cl2], to cleave disulfide bonds in GSSG.
- To characterize the reaction kinetics and products of the interaction between [Pt(Met)Cl2] and GSSG.
Main Methods:
- Electrospray mass spectrometry (ESI-MS)
- High-performance liquid chromatography (HPLC)
- Ultraviolet (UV) spectroscopy
- Kinetic studies at physiological conditions (310 K, pH 7.4)
Main Results:
- The second-order rate constant for [Pt(Met)Cl2] with GSSG was determined as 0.4 M⁻¹s⁻¹, which is 100-fold faster than cisplatin.
- Mono- and dinuclear platinum complexes with GSSG cleavage fragments were identified.
- [Pt(Met)Cl2] was shown to effectively promote disulfide bond cleavage in GSSG.
Conclusions:
- The platinum(II) complex [Pt(Met)Cl2] efficiently cleaves disulfide bonds in oxidized glutathione.
- The findings provide mechanistic insights into the interaction of platinum complexes with cellular redox systems, particularly the glutathione/oxidized glutathione couple.
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