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Thiolation and Carboxylation of Glutathione Synergistically Enhance Its Lead-Detoxification Capabilities
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SYSNO ASEP 0550071 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Thiolation and Carboxylation of Glutathione Synergistically Enhance Its Lead-Detoxification Capabilities Author(s) Sauser, L. (CH)
Mohammed, T. A. (CH)
Kalvoda, Tadeáš (UOCHB-X) ORCID
Feng, S.-J. (CH)
Spingler, B. (CH)
Rulíšek, Lubomír (UOCHB-X) RID, ORCID
Shoshan, M. S. (CH)Source Title Inorganic Chemistry. - : American Chemical Society - ISSN 0020-1669
Roč. 60, č. 24 (2021), s. 18620-18624Number of pages 5 s. Language eng - English Country US - United States Keywords amino acids ; binding energy ; carboxylation OECD category Physical chemistry Method of publishing Limited access Institutional support UOCHB-X - RVO:61388963 UT WOS 000753447800010 EID SCOPUS 85120737256 DOI 10.1021/acs.inorgchem.1c03030 Annotation The natural tripeptide glutathione (GSH) is a ubiquitous compound harboring various biological tasks, among them interacting with essential and toxic metal ions. Yet, although weakly binding the poisonous metal lead (Pb), GSH poorly detoxifies it. β-Mercaptoaspartic acid is a new-to-nature novel amino acid that was found to enhance the Pb-detoxification capability of a synthetic cyclic tetrapeptide. Aiming to explore the advantages of noncanonical amino acids (ncAAs) of this nature, we studied the detoxification capabilities of GSH and three analogue peptides, each of which contains at least one ncAA that harbors both free carboxylate and thiolate groups. A thorough investigation that includes in vitro detoxification and mechanistic evaluations, metal-binding affinity, metal selectivity, and computational studies shows that these ncAAs are highly beneficial in additively enhancing Pb binding and reveals the importance of both high affinity and metal selectivity in synergistically reducing Pb toxicity in cells. Hence, such ncAAs join the chemical toolbox against Pb poisoning and pollution, enabling peptides to strongly and selectively bind the toxic metal ion. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2022 Electronic address https://doi.org/10.1021/acs.inorgchem.1c03030
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