I-Corps: Plasma-based Protein Footprinting
I-Corps: Plasma-based Protein Footprinting
批准号:
1801928
负责人:
Benjamin Minkoff
金额:
$5.0万
依托单位国家:
美国
项目类别:
Standard Grant
财政年份:
2018
资助国家:
美国
项目状态:
已结题
起止时间:
2018-01-01 至 2019-06-30
中文摘要
I-Corps的更广泛的影响/商业潜力将使基于蛋白质的治疗药物(如抗体和生物仿制药)的开发更快。核心技术允许更快地确定此类蛋白质治疗剂的结构特征,这很重要,因为结构对于蛋白质治疗剂的功能和效率都是必不可少的。该技术可以应用于治疗药物开发的许多方面,从最初的发现和筛选阶段到在各种条件和环境下测试开发的治疗药物的稳定性以进行质量控制。鉴于蛋白质疗法的重要部分,特别是在快速增长的生物制药市场中,我们相信我们的技术将对该行业具有重要价值,并能在未来更快地开发治疗疾病的疗法。I-Corps项目进一步开发了一种技术,可以确定液体环境中蛋白质的结构特征。 这是重要的,不仅因为蛋白质的结构决定了它的功能,并且通过了解结构获得了关于蛋白质本身的许多信息,而且还因为蛋白质天然存在于液体环境中的细胞内。等离子体用于从蛋白质周围的水中产生反应分子,通过测量蛋白质上标记有该分子的区域,可以可视化蛋白质的相关区域。当添加改变蛋白质结构或结合并掩蔽蛋白质的一侧/面的另一种元素时,这反映为反应性分子改变修饰的水平或区域。通过这种方式,该技术可以快速绘制蛋白质结构变化。
英文摘要
The broader impact/commercial potential of this I-Corps will be to enable faster development of protein-based therapeutic drugs, such as antibodies and biosimilars. The core technology allows for faster determination of structural features of such protein therapeutic agents, which is important because structure is essential to both the function and efficiency of a protein therapeutic. The technology can be applied at many points within a therapeutic's development, from the initial discovery and screening phases to testing a developed therapeutic's stability under a wide array of conditions and environments for quality control purposes. Given the significant fraction of protein therapeutics, specifically, within the rapidly growing biopharmaceutical market, we believe our technology will both be of significant value to this industry and enable faster development of therapeutics for treating diseases in the future.This I-Corps project further develops a technology that determines structural features of proteins in a liquid environment. This is significant not only because a protein's structure dictates its function and by learning about the structure much information is gained about the protein itself, but also because proteins natively exist within cells in liquid environments. A plasma is used to create a reactive molecule from water surrounding the protein, and by measuring the areas on the protein that get labeled with this molecule, one can visualize relevant regions of the protein. When another element is added that changes the structure of the protein, or binds to and masks one side/face of the protein, this is reflected is changing levels or areas of modification by the reactive molecule. In this way, the technique can quickly map protein structural changes.
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会议论文
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