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目的 确认固相合成多肽P14分子是否存在异构体。方法 通过HP 110 0与ESI离子源PEAPI2 0 0 0液质联用 (LC/MS)分离P14肽 ,在质谱鉴定合成肽主峰为理论设计分子量前提下 ,应用PESCIEXAn alyst 1.0b3质谱分析软件分析子离子流色谱图。结果 从总离子流色谱图中精确提取P14肽Q1正离子双电荷质量数 ,形成P14肽质量数子离子流色谱图 ,其中有散在的不同保留时间的质量数存在。结论 P14肽有异构体存在 ,与结合理论上分析P14氨基酸组成发现 (P14组成中有 6个胱氨酸 ,其存在无疑增加了分子内二硫键形成的可能性 )一致
Objective To confirm the existence of isomers of the P14 molecule of the solid phase synthetic peptide. Methods The P14 peptide was separated by liquid chromatography-mass spectrometry (PE / MS) with HP 110 0 and ESI source PEAPI2 0 0 0. Under the premise of mass spectrometry identification of the main peak of the synthesized peptide as theoretical design molecular weight, PESCIEXAn alyst 1.0b3 mass spectrometry software was used to analyze the molecular ions Chromatogram. Results The double-charge mass of Q1 positive ion of P14 peptide was extracted exactly from the total ion chromatogram to form the mass ion current chromatogram of P14 peptide, in which scattered masses with different retention times existed. Conclusions The P14 peptide is present in an isomeric form, consistent with the theoretical analysis of the P14 amino acid composition (6 cystines in P14 composition, which undoubtedly increases the possibility of intramolecular disulfide bond formation)