课题基金 / 基金详情

RUI: The chemical basis for protein self-assembly and polymerization

RUI: The chemical basis for protein self-assembly and polymerization
RUI:蛋白质自组装和聚合的化学基础
批准号:
1243656
负责人:
Robert Fairman
金额:
$49.25万
依托单位:
依托单位国家:
美国
项目类别:
Standard Grant
财政年份:
2013
资助国家:
美国
项目状态:
已结题
起止时间:
2013-08-01 至 2018-06-30

项目摘要

项目成果

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中文摘要
翻译
在这个项目中,PI试图基于一个扩展的多肽模板和卟啉结构工具包来发现新的生物材料,以创建具有光电活性的纳米线。这些多肽被设计成基于卷曲-螺旋蛋白结构基序形成聚合物,并且产生这些聚合物的能力已经得到很好的证实。这些基于多肽的支架被设计成结合带负电荷的卟啉,利用定义明确的离子相互作用。这项研究的目的是通过扩展设计原则,将带正电的卟啉和卟啉与已结合的金属结合起来,从而显著提高这些材料的实用性。这种设计的扩展将允许增加光电活动的多样性,并允许调节这种活动的能力。在一个新的方向上,一种天然的盘绕结构将被测试为结合卟啉的支架。研究人员将使用肌球蛋白II杆状结构域中的卷曲线圈,将蛋白质共价支架的长度从数十个氨基酸延伸到数百个氨基酸。如果成功,这样的支架将增加可用于制造纳米线的长度尺度。该项目具有高度的跨学科性质,将有助于推进许多不同的活跃研究领域,包括:(1)阐明蛋白质折叠的一般规则和了解聚合过程;(2)设计具有光电子活性的生物材料;以及(3)创造可沉积在表面上用于测试光电子行为的生物材料。这里描述的工作将主要由本科生推动。生物和化学专业的学生将在生物化学和生物物理学领域接受广泛的培训。研究工作的许多方面,特别是蛋白质化学和蛋白质设计,已被纳入PI教授的几门课程。国际和平协会长期致力于改善代表性不足群体获得研究的机会。他参与了几个全学院范围的项目,以提供这种机会,包括:(1)在暑期桥牌项目中任教;(2)监督和指导在周六项目中任教的哈弗福德学生,该项目为来自费城的高中和中学生提供进入学院实验室的机会;以及(3)参与开发新的学术资源办公室,旨在为进入哈弗福德的分析和批判性推理技能较差的学生提供支持。最近,这位调查员在社区中担任领导角色,管理学生和教师研究的资金,并在整个机构内总体上促进和增强教师的学术抱负。该项目由分子和细胞生物科学部的分子生物物理组和化学部的生命过程化学项目共同支持。
英文摘要
In this project the PI seeks to discover novel biomaterials based on an expanding toolkit of peptide templates and porphyrin structures to create photoelectronically active nanowires. The peptides are designed to form polymers based on the coiled-coil protein structural motif, and the ability to generate these polymers is well established. These peptide-based scaffolds have been engineered to bind negatively charged porphyrins, taking advantage of well-defined ionic interactions. This research aims to significantly advance the utility of these materials by expanding the design principles to include binding of positively charged porphyrins and porphyrins with metals that have been incorporated. This expansion in design will allow for increased diversity of photoelectronic activity, and for the ability to modulate this activity. In a new direction, a natural coiled-coil structure will be tested as a scaffold for porphyrin binding. The investigator will use the coiled coil from the rod domain of myosin II to extend the lengths of the protein covalent scaffolds from the range of tens of amino acids to many hundreds of amino acids. If successful, such a scaffold will increase the length scale available for creating nanowires. This project is highly interdisciplinary in nature and will contribute to the advancement of a number of different active fields of research, including: (1) elucidating general protein folding rules and understanding polymerization processes; (2) designing photoelectronically active biomaterials; and (3) creating biomaterials that can be deposited onto surfaces for testing photoelectronic behavior. The work described here will be driven primarily by undergraduates. Biology and chemistry students will receive broad training in the areas of biochemistry and biophysics. Many aspects of the research work, focusing particularly on protein chemistry and protein design, have been incorporated in several courses that the PI teaches. The PI has a longstanding commitment to improving access to research for under-represented groups. He has been involved in several College-wide programs to provide this access, including: (1) teaching in a summer bridge program; (2) supervising and mentoring Haverford students who teach in a Saturday program that provides access to the College laboratories to high school and middle school students from Philadelphia; and (3) participating in the development of a new Office of Academic Resources, designed to provide support for students who enter with weaker skills in analytical and critical reasoning. More recently this investigator has taken leadership roles in the community for stewarding funding for student and faculty research, and generally promoting and enhancing faculty scholarly ambitions across the institution. This project is jointly supported by the Molecular Biophysics Cluster in the Division of Molecular and Cellular Biosciences and by the Chemistry of Life Processes Program in the Chemistry Division.
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