关键词: D-amino acid-containing peptide chirality high-resolution mass spectrometry higher-energy collisional dissociation

Mesh : Tandem Mass Spectrometry / methods Liraglutide Amino Acids / chemistry Peptides / chemistry

来  源:   DOI:10.3390/ijms25031379   PDF(Pubmed)

Abstract:
D-amino acid-containing peptides (DAACPs) occur in biological and artificial environments. Since the importance of DAACPs has been recognized, various mass spectrometry-based analytical approaches have been developed. However, the capability of higher-energy collisional dissociation (HCD) fragmentation to characterize DAACP sites has not been evaluated. In this study, we compared the normalized spectra intensity under different conditions of HCD and used liraglutide along with its DAACPs as examples. Our results indicated that the difference in the intensity of y ions between DAACPs and all-L liraglutide could not only distinguish them but also localize the sites of D-amino acids in the DAACPs. Our data demonstrate the potential of using HCD for the site characterization of DAACPs, which may have great impact in biological studies and peptide drug development.
摘要:
含D-氨基酸的肽(DAACPs)存在于生物和人工环境中。由于认识到DAACP的重要性,已经开发了各种基于质谱的分析方法。然而,尚未评估高能碰撞解离(HCD)碎片表征DAACP位点的能力。在这项研究中,我们比较了不同HCD条件下的归一化光谱强度,并以利拉鲁肽及其DAACPs为例。我们的结果表明,DAACPs和全L利拉鲁肽之间的y离子强度差异不仅可以区分它们,而且可以定位DAACPs中D-氨基酸的位点。我们的数据证明了使用HCD进行DAACP位点表征的潜力,这可能对生物学研究和多肽药物开发产生重大影响。
公众号