Enhancement of solubility by temporary dimethoxybenzyl-substitution of peptide bonds. Towards the synthesis of defined oligomers of alanine and of lysyl-glutamyl-glycine.

J Blaakmeer, T Tijsse-Klasen, G I Tesser
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Abstract

The synthesis of the model compound Aloc-Ala-Ala-Dma-Ala-Ala-OMe has been described as an illustration of the fact that a large group reversibly alkylating the amido group of an oligomer can disturb the regularity of a peptide backbone, oppose its aggregation and thus enhance its solubility greatly, affording synthons for further oligomerization. Application of such a group not only affects the solubility, but alters also the properties of the intermediates. The concomitant change in reactivity may run to such an extent that N-alkylation of oligomers has to be abandoned (this was encountered in the attempted synthesis of Lys-Glu-Dmg). Consequently, the solubility of the growing protected peptide chain will become progressively less and in the mentioned example the oligomerization had to be terminated at the dodecapeptide level, indicating the severe need for reversible "structure-breaking" functions.

暂时二甲氧基苄取代肽键提高溶解度。合成丙氨酸和赖氨酸-谷氨酰-甘氨酸的低聚物。
模型化合物Aloc-Ala-Ala-Dma-Ala-Ala-OMe的合成说明了一个事实,即大基团可逆地烷基化低聚物的胺基可以扰乱肽主链的规律性,反对其聚集,从而大大提高其溶解度,为进一步的低聚提供了合成子。这种基团的应用不仅影响了中间体的溶解度,而且改变了中间体的性质。伴随的反应性变化可能会达到这样的程度,低聚物的n -烷基化必须放弃(这是在尝试合成Lys-Glu-Dmg时遇到的)。因此,不断增长的受保护肽链的溶解度将逐渐降低,并且在上述示例中,寡聚化必须在十二肽水平终止,这表明严重需要可逆的“结构破坏”功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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