CAREER: The Behavior of Proteins at the Solid-Liquid Interface Monitored in situ with Infrared-Visible Sum Frequency Generation: Investigating the Role of Interfacial Water

职业:利用红外-可见光和频生成原位监测固-液界面蛋白质的行为:研究界面水的作用

基本信息

  • 批准号:
    0094332
  • 负责人:
  • 金额:
    $ 48.2万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
    Standard Grant
  • 财政年份:
    2001
  • 资助国家:
    美国
  • 起止时间:
    2001-04-01 至 2006-03-31
  • 项目状态:
    已结题

项目摘要

This CAREER project addresses the molecular level structure of water at the liquid solid interface in the presence of adsorbed protein molecules. Professor Paul Cremer and his coworkers at Texas A&M, with the support of the Analytical and Surface Chemistry Program, will examine the interactions of water, protein molecules, and solid silica surfaces. An understanding of these types of systems is important to a variety of applications, including biocompatibility, biofouling in the food and pharmaceutical industries, and in the development of biosensors and catalysts. Infrared-visible sum frequency generation methods will be used to probe the structure of substrate associated water in the presence of adsorbed protein. Time resolved studies will be implemented to follow structural changes upon adsorption of protein molecules at the solid surface. Educational aspects of this project include the development of a bio-physical chemistry course for upper level undergraduates, and the implementation of undergraduate research projects in the field of protein surface interactions. The interaction of protein molecules with surfaces is important in the development of biosensors, in enhancing biocompatibility for medical implants, and for understanding the process of biofouling in food and pharmaceutical process machinery. The structure of adsorbed water in these systems provides the detailed information that can be used to design surfaces with desired protein adsorption properties. This CAREER project uses state of the art surface spectroscopic methods to probe this structural question. Integration of this basic research with educational goals in the training of bio-physical scientists and in the development of course materials in this area is the focus of the educational aspect of this project.
这个CAREER项目解决了在存在吸附蛋白质分子的情况下,水在液固界面的分子水平结构。 教授保罗克雷默和他的同事在得克萨斯州A M,与分析和表面化学计划的支持下,将检查水,蛋白质分子和固体二氧化硅表面的相互作用。 了解这些类型的系统是很重要的各种应用,包括生物相容性,在食品和制药行业的生物污垢,并在生物传感器和催化剂的发展。 可见光和频产生方法将用于探测在吸附蛋白存在下底物缔合水的结构。 将实施时间分辨研究,以跟踪蛋白质分子在固体表面吸附后的结构变化。 该项目的教育方面包括为高水平本科生开发生物物理化学课程,以及在蛋白质表面相互作用领域实施本科生研究项目。蛋白质分子与表面的相互作用在生物传感器的开发、增强医疗植入物的生物相容性以及理解食品和制药加工机械中的生物污染过程中是重要的。 在这些系统中的吸附水的结构提供了详细的信息,可用于设计具有所需的蛋白质吸附性能的表面。 这个CAREER项目使用最先进的表面光谱方法来探测这个结构问题。 将这一基础研究与生物物理科学家培训和这一领域课程教材编制的教育目标相结合,是该项目教育方面的重点。

项目成果

期刊论文数量(0)
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会议论文数量(0)
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Paul Cremer其他文献

GLIDE Score: A Scoring System for Prediction of Procedural Success in Tricuspid Valve Transcatheter Edge-to-Edge Repair.
GLIDE 评分:用于预测三尖瓣经导管边对边修复手术成功率的评分系统。
  • DOI:
    10.1016/j.jcmg.2024.04.008
  • 发表时间:
    2024
  • 期刊:
  • 影响因子:
    0
  • 作者:
    M. Gerçek;Akhil Narang;M. I. Körber;K. Friedrichs;J. Puthumana;Maria Ivannikova;Mohamed Al;Paul Cremer;Abigail S. Baldridge;Zhiying Meng;P. Luedike;James D. Thomas;T.K. Rudolph;Tobias Geisler;Tienush Rassaf;Roman Pfister;Volker Rudolph;Charles J. Davidson
  • 通讯作者:
    Charles J. Davidson
Feasibility of Non-Invasive Screening for Coronary Allograft Vasculopathy with Positron Emission Tomography Derived Myocardial Blood Flow Assessment
  • DOI:
    10.1016/j.cardfail.2019.07.531
  • 发表时间:
    2019-08-01
  • 期刊:
  • 影响因子:
  • 作者:
    Zarina Sharalaya;Andrew Noll;Paul Cremer;Randall C. Starling;W.H. Wilson Tang
  • 通讯作者:
    W.H. Wilson Tang
GENDER SPECIFIC FACTORS ASSOCIATED WITH MAJOR ADVERSE CARDIOVASCULAR EVENTS: INSIGHTS FROM ACCELERATE
  • DOI:
    10.1016/s0735-1097(18)30743-5
  • 发表时间:
    2018-03-10
  • 期刊:
  • 影响因子:
  • 作者:
    Peta King;Paul Cremer;Stephen Nicholls;A. Lincoff;Venu Menon;Jeffrey Riesmeyer;Giacomo Ruotolo;Julie St John;Ellen McErlean;Steven Nissen
  • 通讯作者:
    Steven Nissen
TCT-74 Baseline Left Ventricular Hypertrophy and 5-Year Outcomes after Transcatheter Aortic Valve Replacement: An Analysis of the PARTNER Trials and Registries
  • DOI:
    10.1016/j.jacc.2019.08.112
  • 发表时间:
    2019-10-01
  • 期刊:
  • 影响因子:
  • 作者:
    Holly Gonzales;Pamela Douglas;Philippe Pibarot;Rebecca Hahn;Omar Khalique;Wael Jaber;Paul Cremer;Neil Weissman;Federico Asch;Yiran Zhang;Zachary Gertz;Sammy Elmariah;Marie-Annick Clavel;Vinod Thourani;Melissa Daubert;Maria Alu;Martin Leon;Brian Lindman
  • 通讯作者:
    Brian Lindman
IMPLICATIONS OF WORSENING RIGHT VENTRICULAR FUNCTION FOLLOWING TRANSCATHETER OR SURGICAL AORTIC VALVE REPLACEMENT: INSIGHTS FROM PARTNER2A
  • DOI:
    10.1016/s0735-1097(17)34355-3
  • 发表时间:
    2017-03-21
  • 期刊:
  • 影响因子:
  • 作者:
    Paul Cremer;L. Leonardo Rodriguez;Yiran Zhang;Maria Alu;Brian Lindman;Alan Zajarias;Rebecca Hahn;Stamatios Lerakis;S. Chris Malaisrie;Pamela Douglas;Philippe Pibarot;Lars Svensson;Martin Leon;Wael Jaber
  • 通讯作者:
    Wael Jaber

Paul Cremer的其他文献

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{{ truncateString('Paul Cremer', 18)}}的其他基金

Rules for Ion Pairing in Aqueous Interfacial Structures
水界面结构中离子对的规则
  • 批准号:
    2305129
  • 财政年份:
    2023
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Standard Grant
Collaborative Research: Ion Mobility in Aqueous Acids, Bases, and Salts
合作研究:酸、碱和盐水溶液中的离子淌度
  • 批准号:
    2154651
  • 财政年份:
    2022
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Standard Grant
Hydrophobic and Electrostatic Driving Forces for Ion Adsorption to Polymers and Extended Interfaces
离子吸附到聚合物和扩展界面的疏水和静电驱动力
  • 批准号:
    2004050
  • 财政年份:
    2020
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Standard Grant
PFI-TT: A High-Throughput Instrument for Measuring the Stability of Liquid Formulations of Therapeutic Proteins
PFI-TT:用于测量治疗性蛋白质液体制剂稳定性的高通量仪器
  • 批准号:
    1919083
  • 财政年份:
    2019
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Standard Grant
INFEWS: N/P/H20: From Antinutrients to Water Pollutants: Exploring the Behavior of Polyphosphate Anions in Aqueous Solutions
INFEWS:N/P/H20:从抗营养剂到水污染物:探索多磷酸根阴离子在水溶液中的行为
  • 批准号:
    1709735
  • 财政年份:
    2017
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Continuing Grant
Investigating the Interactions of Ions with Polypeptides
研究离子与多肽的相互作用
  • 批准号:
    1413307
  • 财政年份:
    2014
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Standard Grant
Probing Protein-Salt Interactions with Microfluidics and Nonlinear Optics
利用微流体和非线性光学探测蛋白质-盐相互作用
  • 批准号:
    0809854
  • 财政年份:
    2008
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Continuing Grant
NSF-NATO POSTDOCTORAL FELLOWSHIPS
NSF-北约博士后奖学金
  • 批准号:
    9633841
  • 财政年份:
    1996
  • 资助金额:
    $ 48.2万
  • 项目类别:
    Fellowship Award

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基因编码的脂化作用可操纵蛋白质的结构、组装和相行为
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