Towards enhanced control of the dissociation chemistry of peptides

加强对肽解离化学的控制

• 批准号: 1403262
• 负责人: Nicolas Polfer
• 金额: $ 43.6万
• 依托单位: University of Florida
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2014
• 资助国家: 美国
• 起止时间: 2014-07-01 至 2019-06-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1403262&HistoricalAwards=false
• 关键词: Towards; enhanced; control; dissociation; chemistry

Professor Nicolas C. Polfer of the University of Florida is supported by the Chemical Measurement and Imaging (CMI) Program in the Division of Chemistry to study the chemistry that takes place when proteins are analyzed by mass spectrometry. The project will expand the scope and improve the fidelity of mass spectrometric characterization of the fragmentation patterns of peptide ions generated from parent proteins. This, in turn, improves the reliability of the high throughput identifications of proteins in complex biological samples. Advances in life sciences depend on the integration of reliable protein identification results with complimentary genomic and metabolomic information. In this context, the project will provide new avenues for the identification of proteins and hence advance our understanding of life processes. In addition, the spectroscopic techniques developed in this work may also lead to applications in other areas of chemistry, such as mechanistic organic chemistry.The analytical mass spectrometric and spectroscopic methods the research team is developing are focused on probing the chemistry that takes place when peptides are fragmented by collision-induced dissociation (CID) for the purpose of peptide and protein sequencing by mass spectrometry. Analytical laser spectroscopy techniques, in particular infrared multiphoton dissociation (IRMPD) and two-laser pump-probe schemes in a cryogenically-cooled 3-D ion trap, will be employed to: 1) provide a deeper understanding of labile and radical rearrangement chemistries that take place, 2) study the dynamics of these rearrangement reactions, and 3) develop methodologies that enable more control in the dissociation chemistry, for improved structural determination of peptides and proteins. The proposed research is of significance to de novo protein sequencing and for the location of posttranslational modifications on the peptide sequence. In the course of this research, graduate students are being trained in state-of-the-art mass spectrometric and spectroscopic techniques. The technologies and the results of the proposed research will be communicated to high school students through workshops aimed at high school science teachers.

佛罗里达大学的Nicolas C. Polfer教授得到化学系化学测量与成像（CMI）项目的支持，研究用质谱法分析蛋白质时发生的化学反应。该项目将扩大范围，提高质谱表征亲本蛋白产生的肽离子碎片模式的保真度。这反过来又提高了复杂生物样品中蛋白质高通量鉴定的可靠性。生命科学的进步依赖于可靠的蛋白质鉴定结果与互补的基因组和代谢组学信息的整合。在这种情况下，该项目将为鉴定蛋白质提供新的途径，从而促进我们对生命过程的理解。此外，在这项工作中发展的光谱技术也可能导致在化学的其他领域的应用，如机械有机化学。研究小组正在开发的分析质谱和光谱方法，主要是为了通过质谱测定肽和蛋白质的序列，探测肽通过碰撞诱导解离（CID）破碎时发生的化学反应。分析激光光谱技术，特别是红外多光子解离（IRMPD）和低温冷却3- d离子阱中的双激光泵浦探针方案，将用于：1)提供对发生的不稳定和自由基重排化学的更深入了解，2)研究这些重排反应的动力学，以及3)开发能够更好地控制解离化学的方法，以改进肽和蛋白质的结构测定。本研究对蛋白质从头测序和肽序列翻译后修饰的定位具有重要意义。在这项研究的过程中，研究生们正在接受最先进的质谱和光谱技术的培训。所建议的研究技术和结果将通过针对高中科学教师的研讨会传达给高中学生。

项目成果

Linkage and Anomeric Differentiation in Trisaccharides by Sequential Fragmentation and Variable-Wavelength Infrared Photodissociation

• DOI: 10.1007/s13361-014-1025-6
• 发表时间: 2015-02
• 期刊: Journal of The American Society for Mass Spectrometry
• 影响因子: 3.2
• 作者: Yanglan Tan;N. Polfer

Insights into the fragmentation pathways of gas-phase protonated sulfoserine

气相质子化磺丝氨酸的裂解途径的见解

• DOI: 10.1016/j.ijms.2014.12.001
• 发表时间: 2015
• 期刊: International Journal of Mass Spectrometry
• 影响因子: 1.8
• 作者: Patrick, Amanda L.;Stedwell, Corey N.;Schindler, Baptiste;Compagnon, Isabelle;Berden, Giel;Oomens, Jos;Polfer, Nicolas C.
• 通讯作者: Polfer, Nicolas C.

H 2 SO 4 and SO 3 Transfer Reactions in a Sulfopeptide-Basic Peptide Complex

硫肽-碱性肽复合物中的 H 2 SO 4 和 SO 3 转移反应

• DOI: 10.1021/acs.analchem.5b02479
• 发表时间: 2015
• 期刊: Analytical Chemistry
• 影响因子: 7.4
• 作者: Patrick, Amanda L.;Polfer, Nicolas C.
• 通讯作者: Polfer, Nicolas C.