High impact information on methoxymethanimidamide

• Lysine epsilon-amino groups of human factor H were selectively converted to guanidino groups by treatment with 0.1 M O-methylisourea at pH 10 [1].
• 1. Erabutoxins, a, b and c, neurotoxic proteins of a sea snake Lacticauda semifasciata, were guanidinated with O-methylisourea [2].
• After conversion of the p-bromobenzyl ether 50 to azide 54, activation of the cyclic urea as its O-methylisourea and reduction of the azide led to spontaneous cyclization to afford the tricyclic nucleus 59 of cylindrospermopsin [3].
• Lys-15 of BPTI was protected by trypsin bound to BPTI, then O-methylisourea (OMIU) was used to guanidinate all unprotected lysines [4].
• Reduced guanidinated RNase, in which most of the lysines are blocked by guanidination with O-methylisourea, also reacts rapidly with BQ, but only ca. 16 equiv are consumed; of these, 8 become covalently bound to protein-SH groups while the others are reduced to HQ [5].

Biological context of methoxymethanimidamide

• Enzymatic hydrolysis of the following compounds could not be detected: phenyl formate, p-nitroformanilide, trifluoroacetamide, p-nitrophenyl carbamate, thiourea, and O-methylisouronium ion [6].
• Acylation of the amino groups of lactoferrin also significantly reduced the interaction with B lymphocytes, and an O-methylisourea treatment of the amino groups, which preserved the positive charge, hardly affected the interaction [7].

Associations of methoxymethanimidamide with other chemical compounds

• Next, O-methylisourea was used to convert lysine residues to homoarginine to increase the sequence coverage, and MALDI-TOF mass spectrometry detection was performed [8].
• Basis of thermostability in pig heart lactate dehydrogenase treated with O-methylisourea [9].

Analytical, diagnostic and therapeutic context of methoxymethanimidamide

• Guanidination performed with isotopic isoforms of O-methylisourea was used in combination with reversed-phase liquid chromatography (LC) matrix-assisted laser desorption/ionization to characterize, both qualitatively and quantitatively, protein mixtures [10].

References