Proteinase resistance of carnosine, pyrrolylcarnosine, and salicylcarnosine

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The stability of carnosine, pyrrolylcarnosine (PC) and salicylcarnosine (SC) to the action of leucine aminopeptidase, carboxypeptidases B and Y was evaluated. It was found that proteolysis of carnosine, PC and SC under the action of leucine aminopeptidase does not occur. Carboxypeptidases B and Y, as well as the enzyme system of blood plasma and plasma membranes of rat brain cells, degraded peptides containing β-alanyl, N-pyrrolyl, N-salicylic fragments to varying degrees. In all cases, histidine is formed. The formation of pyrrole or salicylic acid does not occur. It was found that carnosine, PC and SC showed high stability to the action of amino- and carboxypeptidases in in vitro experiments.

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K. Shevchenko

National Research Centre “Kurchatov Institute”

编辑信件的主要联系方式.
Email: ATCarma@mail.ru
俄罗斯联邦, 123182, Moscow, pl. Kurchatova 2

I. Nagaev

National Research Centre “Kurchatov Institute”

Email: ATCarma@mail.ru
俄罗斯联邦, 123182, Moscow, pl. Kurchatova 2

O. Kulikova

Research Center of Neurology

Email: ATCarma@mail.ru
俄罗斯联邦, 125367, Moscow, Volokolamskoe shosse 80

S. Stvolinsky

Research Center of Neurology

Email: ATCarma@mail.ru
俄罗斯联邦, 125367, Moscow, Volokolamskoe shosse 80

V. Shevchenko

National Research Centre “Kurchatov Institute”

Email: ATCarma@mail.ru
俄罗斯联邦, 123182, Moscow, pl. Kurchatova 2

N. Myasoedov

National Research Centre “Kurchatov Institute”

Email: ATCarma@mail.ru
俄罗斯联邦, 123182, Moscow, pl. Kurchatova 2

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2. Scheme 1. Structural formulas of carnosine (β-alanyl-L-histidine), pyrrolylcarnosine ([3-(N-pyrrolyl)-propanoyl-L-histidine]) and salicylcarnosine ([3-(N-salicyl)-propanoyl-L-histidine]).

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3. Fig. 1. Chromatogram of the PC reaction mixture in the presence of carboxypeptidase B after 24 hours of incubation. PC (retention time 6.80 min), [M + H]+ – 277.2, metabolite (retention time 9.65 min), [M + H]+ – 140.1.

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