EAGER: Elucidating Protein - Colloid Interactions for Enhanced Bio-Energy Applications

EAGER：阐明蛋白质-胶体相互作用以增强生物能源应用

• 批准号: 1242524
• 负责人: Ponisseril Somasundaran
• 金额: $ 9.52万
• 依托单位: Columbia University
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2012
• 资助国家: 美国
• 起止时间: 2012-11-01 至 2013-10-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1242524&HistoricalAwards=false
• 关键词: EAGER; Elucidating; Protein; Colloid; Interactions

PI: Somasundaran, PonisserilProposal Number: 1242524Institution: Columbia UniversityTitle: EAGER: Elucidating Protein - Colloid Interactions for Enhanced Bio-Energy ApplicationsAn emerging trend in alternative energy technologies is the use of enzymes or other functional proteins to generate energy; this can already be seen in bio-fuel efforts, where enzymes are used to break down crystalline cellulose into simpler sugars. More radical approaches to ?bio-energy? include bio-fuel cells, where enzymes are the catalysts that oxidize sugar to generate a current; or bio-solar which takes advantage of photosynthetic proteins to capture and harness photonic energy. The ecological advantages are apparent: enzyme catalyzed processes are low temperature and require no harsh solvents. However, the challenge lies in finding ways of maximizing their stability and function outside of a biological environment.The goal of this EAGER project is to explore the unknown interactions that arise from protein ? colloid interactions; specifically those that enable active portions to seemingly ?perceive? their environment through the protein structure in which they are embedded. Whatever mechanisms responsible for these macromolecular sensory phenomena may be responsible for the synergistic interactions which occur between non-ionic surfactants and enzymes, resulting in increased enzyme activity.PI hypothesizes that surfactant aggregates (micelles) interact with the external structure of enzymes to affect changes in fluctuations, causing sub-angstrom scale dynamic motions which ultimately affect the active site position and range of motion. The PI will study this novel concept through a exploratory research plan - starting with a foundation in comparing enzyme kinetics, to understanding colloid and protein structure behavior, and then molecular dynamic modeling. From these observations, the PI intend to develop a thorough model of the physical interactions that occur between the enzyme structure and surfactants as well as surfactant-aggregates, with the ultimate goal of determining if there is a connection between non-ionic surfactant micelles, enzyme structure flexibility and enzyme activity.This previously unexplored concept attempts to build a bridge between the bulk interactions of enzyme kinetics in crowded colloid systems with the atomic scale motions and forces that dictate elements of protein flexibility and selectivity. Because the PI are seeking to find agreement between two extremes of observable phenomena, a multidisciplinary approach is required; including but not limited to studying the bulk macromolecular phenomena that are indicative of the state of protein structure dynamics, such as reaction kinetics, static structure spectroscopy and colloid physics. The PI will then correlate these findings with investigations with novel techniques in 2d spectroscopy and molecular dynamics modeling to investigate pico-scale spatial and temporal phenomena, stopping short of regions where quantum effects begin to complicate observations.This project has implications for biofuel and for several fields outside of alternative energy, such as: home-personal care, waste management and medicine, possibly reducing the chemicals consumed for various applications by taking advantage of synergies between them and protein structural conformation dynamics. The PI will use this project to train and engage undergraduate students, particularly those from targeted groups, who have become attracted to such Green projects. In as much as this has yet to be substantiated, this broad interdisciplinary scope of investigation, coupled with emerging instrumental techniques, and prospective implications to the tangent fields mentioned above, mark this project as a ?high risk and high reward? situation, and an appropriate EAGER submission.

PI：Somasundaran，Ponisseril 提案编号：1242524 机构：哥伦比亚大学 标题：EAGER：阐明蛋白质 - 胶体相互作用以增强生物能源应用替代能源技术的一个新兴趋势是使用酶或其他功能性蛋白质来产生能量；这已经可以在生物燃料的研究中看到，其中酶被用来将结晶纤维素分解成更简单的糖。更激进的“生物能源”方法包括生物燃料电池，其中酶是氧化糖以产生电流的催化剂；或生物太阳能，利用光合蛋白质来捕获和利用光子能。生态优势显而易见：酶催化过程温度低且不需要刺激性溶剂。然而，挑战在于找到在生物环境之外最大化其稳定性和功能的方法。这个 EAGER 项目的目标是探索蛋白质产生的未知相互作用？胶体相互作用；特别是那些使活跃部分看似“感知”的部分通过它们所嵌入的蛋白质结构来了解它们的环境。无论导致这些大分子感觉现象的机制是什么，都可能导致非离子表面活性剂和酶之间发生的协同相互作用，从而导致酶活性增加。PI假设表面活性剂聚集体（胶束）与酶的外部结构相互作用，从而影响酶的变化波动，引起亚埃尺度的动态运动，最终影响活性部位的位置和运动范围。 PI 将通过探索性研究计划来研究这一新概念——从比较酶动力学的基础开始，了解胶体和蛋白质结构行为，然后进行分子动力学建模。根据这些观察结果，PI 打算开发一个关于酶结构与表面活性剂以及表面活性剂聚集体之间发生的物理相互作用的全面模型，最终目标是确定非离子表面活性剂胶束、酶和表面活性剂之间是否存在联系。结构灵活性和酶活性。这个以前未经探索的概念试图在拥挤的胶体系统中酶动力学的整体相互作用与决定蛋白质灵活性和选择性元素的原子尺度运动和力之间建立一座桥梁。由于 PI 正在寻求在可观察现象的两个极端之间找到一致性，因此需要采用多学科方法；包括但不限于研究表明蛋白质结构动力学状态的大分子现象，例如反应动力学、静态结构光谱和胶体物理学。然后，PI 将把这些发现与二维光谱和分子动力学建模中的新技术研究联系起来，以研究皮尺度空间和时间现象，避免量子效应开始使观测变得复杂的区域。该项目对生物燃料和多种生物燃料具有影响。替代能源以外的领域，例如：家庭个人护理、废物管理和医药，通过利用它们与蛋白质结构构象动力学之间的协同作用，可能减少各种应用消耗的化学品。 PI 将利用该项目来培训和吸引本科生，特别是那些对此类绿色项目感兴趣的目标群体学生。尽管这一点尚未得到证实，但这种广泛的跨学科研究范围，加上新兴的仪器技术以及对上述切线领域的预期影响，使该项目成为“高风险和高回报”的项目。情况，以及适当的 EAGER 提交。