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 Proposal编号：1242524机构：哥伦比亚大学标题：EIGER：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蛋白质来产生能量；这已经可以在生物燃料努力中看到，其中酶被用来将结晶纤维素分解成更简单的糖。更激进的方法？生物能源？包括生物燃料电池，酶是氧化糖产生电流的催化剂；或者生物太阳能，它利用光合作用蛋白质来捕获和利用光能。生态优势是显而易见的：酶催化过程温度低，不需要苛刻的溶剂。然而，挑战在于找到使它们在生物环境之外的稳定性和功能最大化的方法。这个渴望的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；特别是那些使活性部分看起来？感知？它们所处的环境通过它们所嵌入的蛋白质结构。无论这些大分子感官现象的机制是什么，都可能是非离子表面活性剂与酶之间发生协同作用，导致酶活性增加的原因。PI假设表面活性剂聚集体(胶束)与酶的外部结构相互作用，影响波动的变化，导致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将通过一项探索性的研究计划来研究这一新概念-从比较酶动力学的基础开始，到了解胶体和蛋白质的结构行为，然后是分子动力学建模。通过这些观察，PI打算开发一个发生在酶结构和表面活性剂以及表面活性剂-聚集体之间的物理相互作用的彻底模型，最终目标是确定非离子表面活性剂胶束、酶结构灵活性和酶活性之间是否存在联系。这一以前未曾探索的概念试图在拥挤的胶体系统中酶动力学的主体相互作用与原子尺度运动和决定蛋白质灵活性和选择性的元素的力之间建立桥梁。由于PI试图在两个极端的可观察现象之间找到一致，因此需要一个多学科的方法；包括但不限于研究指示蛋白质结构动力学状态的主体大分子现象，如反应动力学、静态结构光谱和胶体物理。然后，PI将把这些发现与2D光谱和分子动力学建模中的新技术相关联，以研究微微尺度的空间和时间现象，阻止量子效应开始使观测复杂化的区域。该项目对生物燃料和替代能源以外的几个领域有影响，如：家庭-个人护理、废物管理和医药，可能通过利用它们之间的协同作用和蛋白质结构构象动力学来减少各种应用的化学品消耗。国际学生联合会将利用这一项目来培训和吸引大学生，特别是那些来自目标群体的学生，他们已经被这些绿色项目所吸引。由于这一点尚未得到证实，这种广泛的跨学科调查范围，加上新兴的工具技术，以及对上述切线领域的预期影响，标志着这个项目是一个高风险和高回报的项目。情况，以及适当的急切服从。