the introduction of one or more maleyl groups into a substance by acylation, e.g. with maleic anhydride. Maleylation of a protein with maleic anhydride is used to acylate its free lysine (and other) amino groups in order to change their charge at neutral pH from positive to negative and to render the adjacent peptide bonds resistant to hydrolysis by trypsin; it can also lead to disaggregation of a multimeric protein. The reaction occurs at pH 8.5 (usually at 2°C) and the maleyl groups can be removed at pH 3.5 (usually at 60°C). Maleylation of thiol groups may also occur. Compare citraconylation, succinylation. —maleylatevb.