Benovitz D E, Spatola A F
Peptides. 1985 Mar-Apr;6(2):257-61. doi: 10.1016/0196-9781(85)90049-x.
Five analogs of leucine enkephalin containing the CH2S group as an amide bond replacement were evaluated with respect to resistance toward degradation by human serum in an HPLC-based assay using both ultraviolet and electrochemical detection. Analogs with the modification at the 1-2, 2-3, 3-4, or 4-5 peptide linkages demonstrated half-lives of 118, 85, 134, and 318 min vs. 12 min for the parent peptide. A pseudopeptide analog with additional D-Ala2 protection had a half-life of greater than 1000 min, while the potent [D-Ala2]-leucine enkephalin analog showed approximately a 10-fold increase in stability. The significant increase in stability for a compound with protection only at the C-terminus suggests that serum enzymes may have greater specificity toward backbone changes than previously realized.
在一项基于高效液相色谱（HPLC）的分析中，使用紫外和电化学检测方法，对5种含有CH2S基团作为酰胺键替代物的亮氨酸脑啡肽类似物进行了人血清降解抗性评估。在1-2、2-3、3-4或4-5肽键处进行修饰的类似物，其半衰期分别为118、85、134和318分钟，而母体肽的半衰期为12分钟。具有额外D-Ala2保护的假肽类似物半衰期大于1000分钟，而强效的[D-Ala2]-亮氨酸脑啡肽类似物稳定性增加约10倍。仅在C端具有保护的化合物稳定性显著增加，这表明血清酶对主链变化的特异性可能比之前认识到的更高。
