Yonezawa H, Takahashi N, Ohno M, Izumiya N
Int J Pept Protein Res. 1978 Jan;11(1):19-27. doi: 10.1111/j.1399-3011.1978.tb02816.x.
The decapeptide corresponding to the amino acid sequence of porcine luteinizing hormone-releasing hormone (LH-RH) which involves 1 mol of tryptophan was synthesized via solid phase synthesis with two different deblocking procedures which used hydrogen chloride in formic acid and hydrogen chloride in acetic acid containing 1% 2-mercaptoethanol. After some fundamental studies on the former reagent with respect to deblocking efficiency toward the Boc group, 0.5 M hydrogen chloride (a 10-fold molar excess with respect to the N-terminal Boc group) in formic acid was used in the present synthesis. The two synthetic products exhibited the same chemical and biological properties as an authentic LH-RH. Hydrogen chloride in formic acid has proved effective without a scavenger although loss of peptide from the resin occurred to a somewhat greater extent than that with hydrogen chloride in acetic acid. A derivative of the synthetic LH-RH formylated at the indole nitrogen had a greatly diminished biological activity, indicating that the intact indole side chain is essential for the activity.
通过固相合成法，采用两种不同的脱保护方法合成了与猪促黄体生成激素释放激素（LH-RH）氨基酸序列相对应的十肽，该十肽含有1摩尔色氨酸，两种方法分别使用了甲酸中的氯化氢和含1% 2-巯基乙醇的乙酸中的氯化氢。在对前一种试剂关于Boc基团的脱保护效率进行了一些基础研究之后，本合成中使用了甲酸中的0.5M氯化氢（相对于N端Boc基团有10倍的摩尔过量）。这两种合成产物表现出与天然LH-RH相同的化学和生物学性质。尽管与乙酸中的氯化氢相比，从树脂上损失的肽量稍多，但已证明甲酸中的氯化氢在没有清除剂的情况下是有效的。在吲哚氮上甲酰化的合成LH-RH衍生物的生物活性大大降低，这表明完整的吲哚侧链对活性至关重要。
