ArticleInternational journal of molecular sciences2015
Heavy metal complexation of thiol-containing peptides from soy glycinin hydrolysates.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Development of a 96-Well Plate Dithiothreitol Method for the Colorimetric Determination of Nickel Ions in Water Samples.Sensors (Basel, Switzerland) · 2025Article
- Peptide-Based Inorganic Nanoparticles as Efficient Intracellular Delivery Systems.Pharmaceutics · 2025Review
- Copper-Induced Stimulation of Ectophosphatase Activity ofPathogens (Basel, Switzerland) · 2025Article
- A novel approach for the identification of cadmium-chelating compounds in plant-based foods using SEC-ICP-MS/MS and SEC-QTOF-MS.Analytical and bioanalytical chemistry · 2025Article
- Turning Food Protein Waste into Sustainable Technologies.Chemical reviews · 2023Review
- Lead detoxification of edible fungiFrontiers in nutrition · 2023Article
- Benzylaminopurine and Abscisic Acid Mitigates Cadmium and Copper Toxicity by Boosting Plant Growth, Antioxidant Capacity, Reducing Metal Accumulation and Translocation in Bamboo [Antioxidants (Basel, Switzerland) · 2022Article
- Alleviating Effect of Methionine on Intestinal Development and Intercellular Junction Induced by Nickel.Biological trace element research · 2022Article
- Physiological responses, tolerance, and remediation strategies in plants exposed to metalloids.Environmental science and pollution research international · 2021Review
- A DFT study of isolated histidine interactions with metal ions (NiJournal of molecular modeling · 2020Article
- Selective Extraction and Antioxidant Properties of Thiol-Containing Peptides in Soy Glycinine Hydrolysates.Molecules (Basel, Switzerland) · 2018Article
- Exogenous Glutathione Enhances Mercury Tolerance by Inhibiting Mercury Entry into Plant Cells.Frontiers in plant science · 2017Article
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5 authors.
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Abstract
Many thiol-containing molecules show heavy metal complexation ability and are used as antidotes. In this study, the potential function associated with thiol-containing peptides (TCPs) from soy protein hydrolysates as natural detoxicants for heavy metals is reported. TCPs enriched by Thiopropyl-Sepharose 6B covalent chromatography had different molecular weight distributions as well as different numbers of proton dissociable groups, depending on the proteases and degree of hydrolysis. The major contribution of sulfhydryl groups was confirmed by the largest pH decrease between 8.0 and 8.5 of the pH titration curves. The complexation of TCPs with heavy metals was evaluated by stability constants (βn) of TCP-metal complexes whose stoichiometry was found to be 1:1 (ML) and 1:2 (ML2). TCPs from degree of hydrolysis of 25% hydrolysates gave high affinities towards Hg2+, Cd2+, and Pb2+ (giving similar or even bigger lgβ values than that of glutathione). A significantly positive correlation was found between the logarithm of stability constants for ML2 (lgβ2) and the sulfhydryl group content. Molecular weight distribution of TCPs affected the complexation with Pb2+ notably more than Hg2+ and Cd2+. These results suggest that soy TCPs have the potential to be used in the formulation of functional foods to counteract heavy metal accumulation in humans.
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