Collaborative Research: Intrinsic Gas-phase Properties of Amino Acids and Peptides: Thermochemistry, Fragmentation Mechanisms, H/D exchange and IRMPD Spectroscopy

合作研究：氨基酸和肽的固有气相性质：热化学、断裂机制、H/D 交换和 IMPD 光谱

• 批准号: 1464966
• 负责人: Jennifer Poutsma
• 金额: $ 3万
• 依托单位: Old Dominion University Research Foundation
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2015
• 资助国家: 美国
• 起止时间: 2015-09-01 至 2018-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1464966&HistoricalAwards=false
• 关键词: Collaborative; Research; Intrinsic; Gas; phase

With this award, the Chemical Structure, Dynamics and Mechanisms program is supporting the Collaborative research of Professor John C. Poutsma at the College of William and Mary and Professor Jennifer Poutsma at Old Dominion University. Professor John Poutsma employs mass spectrometry-based experiments to study the subtle interplay between the structure of amino acids and their gas-phase energetic properties. He is studying a class of compounds known as non-protein amino acids (NPAA), which are found naturally in plants and fungi, but are not used in protein synthesis. Many NPAAs are toxic to humans and other animals in part due to structural similarity to one or more of the twenty common protein amino acids (PAA). NPAAs can compete with PAAs in a variety of biological pathways including being mis-incorporated into proteins and peptides. These experiments will further understanding of the intrinsic chemistry of NPAAs as isolated entities and when incorporated into small peptides. Professor Jennifer Poutsma is performing density functional theory calculations that support and guide the experimental studies. Both research programs integrate research and educational components through the training of undergraduate researchers. The vast majority of the research projects outlined in this proposal are being performed by undergraduates at William and Mary and Old Dominion University. Performing independent research helps to teach these students not only the joy of discovery but also how to handle and work though the inevitable failures that accompany real-world science. In this research, the intrinsic gas-phase thermochemical properties of di-peptides are being determined using the extended kinetic method in a triple quadrupole instrument. Specifically, the PIs are studying the gas-phase acid-base chemistry of dipeptides that contain proline or one of its non-protein amino acid analogs azetidine-2-carboxylic acid or pipecolic acid. Thar are working to determine the effects of ring-size and conformational flexibility on the acid-base properties of these species with the goal of applying this knowledge towards a better understanding the mechanisms for selective fragmentations in low-energy tandem mass spectrometry experiments of proline-containing peptides.

有了这个奖项，化学结构，动力学和机制计划是支持教授约翰C。威廉和玛丽学院的普茨玛和老自治领大学的詹妮弗·普茨玛教授。John Poutsma教授采用基于质谱的实验来研究氨基酸结构及其气相能量特性之间的微妙相互作用。他正在研究一类被称为非蛋白质氨基酸（NPAA）的化合物，它们在植物和真菌中天然存在，但不用于蛋白质合成。许多NPAAs对人类和其他动物有毒，部分原因是与二十种常见蛋白质氨基酸（PAA）中的一种或多种结构相似。NPAA可以在多种生物学途径中与PAA竞争，包括错误掺入蛋白质和肽中。这些实验将进一步了解NPAA作为分离实体和掺入小肽时的内在化学。Jennifer Poutsma教授正在进行密度泛函理论计算，以支持和指导实验研究。这两个研究项目通过本科研究人员的培训整合了研究和教育部分。本提案中概述的绝大多数研究项目都是由威廉和玛丽以及旧自治领大学的本科生完成的。进行独立的研究有助于教这些学生不仅发现的乐趣，但也如何处理和工作，虽然不可避免的失败，伴随着现实世界的科学。在这项研究中，固有的气相热化学性质的二肽正在确定使用扩展的动力学方法在三重四极杆仪器。具体来说，PI正在研究含有脯氨酸或其非蛋白质氨基酸类似物氮杂环丁烷-2-羧酸或哌啶酸之一的二肽的气相酸碱化学。Thar正在努力确定环的大小和构象的灵活性对这些物种的酸碱性质的影响，其目标是将这些知识应用于更好地理解含脯氨酸肽的低能串联质谱实验中选择性片段化的机制。