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Non-covalent Complexes

Non-covalent Complexes
非共价配合物
批准号:
0909743
负责人:
Michael Bowers
金额:
$73.0万
依托单位国家:
美国
项目类别:
Standard Grant
财政年份:
2009
资助国家:
美国
项目状态:
已结题
起止时间:
2009-08-01 至 2013-07-31
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中文摘要
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英文摘要
This award is funded under the American Recovery and Reinvestment Act of 2009 (Public Law 111-5). In this award funded by the Experimental Physical Chemistry Program of the Division of Chemistry, Professor Michael Bowers of University of California, Santa Barbara, explores the question of why peptides and proteins in living systems are soley composed of L-amino acids - one of the deepest mysteries in biology. Professor Bowers and his students will start with several simple model systems of peptides that are available in a wide range of chirally mixed forms. These peptides are small enough (5 or 6 amino acids long) that good theory can be done on them to help understand observed changes in their folding and aggregation tendencies as a function of their chiral purity. These peptide families will also provide an entrée into a second major thrust of the proposal - amyloid formation mechanisms. Amyloids are ubiquitous in complex living systems and are implicated in many serious diseases (Alzheimer's, type 2 diabetes, etc.). The goal is to understand the aggregation process and how initially coiled or alpha-helical oligomeric systems end up as large beta-sheet assemblies. As part of this effort Professor Bower's team will initiate a collaboration with Gerhard Meijer and Gert Von Helden at the Fritz Haber Institute in Berlin. This group is building a state of the art instrument to Professor Bower's specifications for this work to couple with a new free electron laser under construction at that facility. Finally the researchers have initiated studies on a related biologically important amyloid system, the 37 residue IAPP or amylin peptide, involved in type 2 diabetes. The human wild type peptide rapidly forms large oligomers but a number of very similar peptides do not. Preliminary data implicate compact assemblies as leading to fibril formation (and hence disease) while elongated assemblies of the same oligomer number do not aggregate further. Modeling and further experiments are planned to fully understand these initial results. Science education in the United States is in a sustained downturn that threatens our world leadership in both innovation and technology development. The problems start early. The 5th grade has been targeted as the first "go" or "no go" indicator in a child's scientific development. At UCSB there is a strong outreach program at the 5th grade level initiated and sustained by a former group member with continuing help from current research group members. Professor Bowers decided to tackle the second "go" or "no go" decision time in young adults - their high school years. His group is developing an outreach program using all group members to present their research projects to high school classes and to relate their personal scientific stories and how they ended up in graduate school at UCSB. A preliminary trial with one of the group members has been run with encouraging results. Additional UCSB faculty and research groups will be incorporated as the program grows.
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SBIR Phase II: A cloud-native, data-driven platform for automated quality assurance of radiation oncology treatment planning
  • 批准号:
    2035750
  • 项目类别:
    Cooperative Agreement
  • 资助金额:
    $100.0万
  • 财政年份:
    2021
  • 负责人:
    Michael Bowers
  • 依托单位:
Assembly and Peptide Cross Talk in Amyloid Systems
SBIR Phase I: A Data-Driven, Knowledge-Based Platform for Peer Review in Radiation Oncology Treatment Planning
  • 批准号:
    1913081
  • 项目类别:
    Standard Grant
  • 资助金额:
    $22.5万
  • 财政年份:
    2019
  • 负责人:
    Michael Bowers
  • 依托单位:
Amino Acid and Peptide Asssembly: Mechanisms and Structures
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