Enzymatic degradation studies of endomorphin-2 and its analogs containing N-methylated amino acids

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• 作者：Anna Janecka ; Rafal Kruszynski ; Jakub Fichna ; Piotr Kosson and Tomasz Janecki
• 关键词：Constrained amino acids ; μ ; -Receptor agonist ; Binding studies ; Enzymatic hydrolysis ; Brain homogenate
• 刊名：Peptides
• 出版年：2006
• 出版时间：January 2006
• 年：2006
• 卷：27
• 期：1
• 页码：131-135
• 全文大小：146 K

文摘

In this paper, we describe the synthesis of novel endomorphin-2 analogs, containing N-methylated amino acids, consecutively in each position. The receptor-binding profile of the new analogs and their stability against enzymatic cleavage by commercially available peptidases, carboxypeptidase Y and aminopeptidase M, and a rat brain homogenate are reported. The best analog of this series, [Sar²]endomorphin-2, was almost equipotent with the parent peptide in the μ-receptor-binding assay and was also highly resistant to enzymatic degradation. This analog may be a suitable candidate for the in vivo antinociceptive studies.