On which amino acids are protein adducts mostly formed?
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Protein adduct formation predominantly occurs on cysteine residues. Various studies have highlighted the significance of cysteine as the primary amino acid involved in the covalent binding of reactive metabolites or compounds like acrylamide, arecoline, and nitrogen mustards to proteins. These adduct formations on cysteine residues have been observed in different contexts, such as drug-protein interactions, food safety concerns, and exposure biomarker identification. The reactivity of cysteine with these compounds leads to the formation of stable adducts, making cysteine a crucial target for adduction. This consistent observation across multiple studies underscores the importance of cysteine residues in protein adduct formation, emphasizing their role as key sites for covalent modifications by various reactive substances.
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30 Citations | Protein adducts are mostly formed on cysteine amino acid residues, but adduction also occurs on lysine and histidine residues with nitrogen mustards mechloroethamine and tris-(2-chlorethyl)amine. |
| Protein adducts are mostly formed on histidine amino acids, specifically τN-(1-MIM)-His and πN-(1-MIM)-His, when exposed to metabolites of 1-methoxy-3-indolylmethyl glucosinolate in vitro and in mouse models. | |
| Protein adducts are mostly formed on cysteine residues, as observed in the study using raloxifene as a model drug for quantifying drug-protein adducts. | |
9 Citations | Protein adducts are predominantly formed on cysteine amino acids when reacting with arecoline and arecaidine, as highlighted in the study. |
| Protein adducts with acrylamide are mostly formed on γ-aminobutyric acid (GABA) among six amino acids studied in the research. |
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