Mass spectrometric and chemical stability of the Asp-Pro bond in herpes simplex virus epitope peptides compared with X-Pro bonds of related sequences
Mass spectrometric and chemical stability of the Asp-Pro bond in herpes simplex virus epitope peptides compared with X-Pro bonds of related sequences
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DOI：
10.1002/psc.395
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发表时间：
2002-08-01
影响因子：
2.1
通讯作者：
Hudecz, F
中科院分区：
文献类型：
--
作者：
Skribanek, Z;Mezo, G;Hudecz, F
对单纯疱疹病毒Ⅰ型（HSV-1）糖蛋白D（gD）免疫优势表位区（273-284）的质谱分析表明，在Asp-Pro肽键上有一个有利的fis离子。对密切相关的X Pro肽的研究证明，肽的长度和氨基酸组成对此都没有显著影响。这些观察结果促使我们比较与gD的273-284表位区域相关的一组新的九肽即SALLEDPVG和SALLEXPVG肽的化学和质谱稳定性，其中X =分别为A K I S F E或D通过电喷雾质谱（ESI MS）研究了这些肽在酸性水解过程中的化学稳定性，并通过ESI MS和在线高效液相色谱-质谱（HPLC MS）鉴定了产物用电喷雾质谱和液相二次离子质谱研究了未经处理的多肽样品的质谱转移和键的稳定性。化学水解和质谱裂解都表明，Asp Pro键在两种情况下都容易断裂，而KP键在两种情况下都是稳定的。（X = A、S、F或E）在质谱条件下容易片段化，但对酸解不敏感。
The mass spectrometric analysis of the immunodominant epitope region (273-284) of herpes simplex virus type I (HSV 1) glycoprotein D (gD) showed a favoured fis ion at the Asp Pro peptide bond The fast atom bombardment collision induced dissociation (FAB CID) study of closely related X Pro peptides documented that neither the length nor the amino acid composition of the peptide has a significant influence on this preferential cleavage At the same time the DP bond proved to be sensitive to acidic conditions in the course of peptide synthesis These observations prompted us to compare the chemical and mass spectrometric stability of a new set of nonapeptides related to the 273-284 epitope region of gD i e SALLEDPVG and SALLEXPVG peptides where X = A K I S F E or D respectively The chemical stability of these peptides during acidic hydrolysis was investigated by electrospray iorn/ation mass spectrometry (ESI MS) and the products were identified by ESI MS and on line high performance liquid chromatography - mass spectrometry (HPLC MS) The mass spectrometric tra(male)mentation and bond stability of the untreated peptide samples were also studied using ES1 MS and liquid secondary ion mass spectrometry (LSIMS) Both the chemical hydrolysis and the mass spectrometric fragmentation showed that the Asp Pro bond could easily be cleaved while the KP bond proved to be stable under both circumstances On the other hand the XP bond (X = A I S F or E) fragmented easily under the mass spectrometric conditions but was not sensitive to the acidolysis Copyright (C) 2002 European Peptide Society and John Wiley Sons Ltd.