| NSF Org: |
DMR Division Of Materials Research |
| Recipient: |
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| Initial Amendment Date: | August 10, 2012 |
| Latest Amendment Date: | August 10, 2012 |
| Award Number: | 1234161 |
| Award Instrument: | Standard Grant |
| Program Manager: |
John Schlueter
jschluet@nsf.gov (703)292-7766 DMR Division Of Materials Research MPS Directorate for Mathematical and Physical Sciences |
| Start Date: | September 1, 2012 |
| End Date: | August 31, 2016 (Estimated) |
| Total Intended Award Amount: | $500,000.00 |
| Total Awarded Amount to Date: | $500,000.00 |
| Funds Obligated to Date: |
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| History of Investigator: |
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| Recipient Sponsored Research Office: |
3451 WALNUT ST STE 440A PHILADELPHIA PA US 19104-6205 (215)898-7293 |
| Sponsor Congressional District: |
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| Primary Place of Performance: |
231 S. 34th Street Philadelphia PA US 19104-6323 |
| Primary Place of
Performance Congressional District: |
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| Unique Entity Identifier (UEI): |
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| Parent UEI: |
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| NSF Program(s): |
OFFICE OF MULTIDISCIPLINARY AC, DMR SHORT TERM SUPPORT, Macromolec/Supramolec/Nano |
| Primary Program Source: |
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| Program Reference Code(s): |
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| Program Element Code(s): |
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| Award Agency Code: | 4900 |
| Fund Agency Code: | 4900 |
| Assistance Listing Number(s): | 47.049 |
ABSTRACT
ID: MPS/DMR/BMAT(7623) 1235084 PI: Pochan, Darrin ORG: University of Delaware
ID: MPS/DMR/BMAT(7623) 1234161 PI: Saven, Jeffrey ORG: University of Pennsylvania
Title: DMREF: Collaborative Research - Programmable peptide-based hybrid materials
TECHNICAL
Biologically-derived proteins and peptides assemble to yield complex structures and functions (e.g. viruses). In contrast, much simpler assemblies typically result (e.g. spherical micelles) when synthetic macromolecules are employed. The sophistication of protein and peptide structures is possible because of their (1) versatile, heteropolymeric chemistry (i.e., amino acid sequences), (2) defined secondary structures (i.e. molecular conformations such as beta-sheets, alpha-helices, and other turns and coils) that provide for specific, local shapes to display amino-acid functionality,(3) well-defined, intramolecular, folded conformations (tertiary structure), and (4) well-ordered quaternary, or intermolecular, structure through the assembly of multiple polypeptide chains. As in nature, the potential exists to build new complex structures and functions via the careful choice of the sequence of amino acids in a polypeptide. This DMREF effort will elucidate fundamental principles and methods for the design of nonnatural one- and two-dimensional polypeptide assemblies. The solution assembly of these designed peptides will be characterized experimentally, and they will be functionalized to realize polypeptide/metal nanoparticle hybrid materials. Theoretical approaches for the design of polypeptide assemblies will be applied and refined in an intimate collaboration with experimental studies. The chemical versatility of peptides will be harnessed to explore and exploit solution assembly processes that are hierarchical, multicomponent, thermodynamically preferred and/or kinetically controlled. Comprehensive nanoscale- through-microscale characterization of the polypeptide assembly, structural intermediates, and final materials will inform future iterations of theory and solution processing. The development of these approaches to materials assembly will facilitate the technological goal of creating robust, solution-assembly methods to produce metal nanoparticle arrays with controlled interparticle spacing and symmetry.
NON-TECHNICAL
This collaborative effort parallels goals of the Materials Genome Initiative. Concepts and methods for predictive materials discovery will be developed in the context of theory-driven design of polypeptides that assemble into targeted materials and nanostructures. New experimental methods for studying and guiding molecular assembly in solution will be refined to monitor polypeptide assembly and to build polypeptide/nanoparticle materials with hierarchical complexity. The close interaction of theory and experiment is essential in the development of a predictive understanding of these materials. The concepts and methods so developed will speed the discovery of new polypeptide-based hybrid materials, and the use of the peptides to specify the arrangement and positioning of metal nanoparticles, has a variety of potential applications, including enhancement of light capture in photovoltaic cells. This collaboration will provide undergraduates, graduate students, and post-doctoral researchers at the University of Delaware and University of Pennsylvania with multidisciplinary knowledge and expertise in the design, modeling, fabrication, and characterization of peptide-based biomaterials. This physical science effort will coordinate with the Interdisciplinary Humanities Research Center at the University of Delaware. Journalism students and faculty associated with the environmental humanities program will work with the DMREF science team. This effort will produce: (1) researchers better trained in communicating science to the general public and in describing the impact of the science and any eventual technology, and (2) future journalists with experience in multidisciplinary research who are skilled in assimilating scientific nuance and complexity into discussions of the research and its impact.
PUBLICATIONS PRODUCED AS A RESULT OF THIS RESEARCH
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PROJECT OUTCOMES REPORT
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This Project Outcomes Report for the General Public is displayed verbatim as submitted by the Principal Investigator (PI) for this award. Any opinions, findings, and conclusions or recommendations expressed in this Report are those of the PI and do not necessarily reflect the views of the National Science Foundation; NSF has not approved or endorsed its content.
Overview: At the molecular scale, nature uses genetically encoded chain molecules, proteins and peptides, to create exquisitely structured assemblies. These biomolecules fold spontaneously to precise structures whose subsequent assembly can be controlled by controlling temperature, chemical modification, and the local solution environment. With proper control over molecular design and supramolecular assembly, peptides offer unlimited potential in the design of new materials that can uniquely address current limitations in the construction of various biomolecular materials and electronic devices. Complex material structures on the dimensions of nanometers can potentially be created that spontaneously form designed lattices, patterns, and assemblies having a wide range of functionalities, e.g, positioning nanometallic components or selective chemically reactive sites; time- and cost-intensive lithographic techniques are not required. This potential capability represents one aspect of a long-standing goal of materials science: how to encode materials structure and properties into the structures and compositions of the constituting molecules.
Intellectual Merit: Proteins and peptides are complex, have enormous numbers of possible molecules (sequences of the amino acids), and can be difficult to work with. To this end we have developed and applied computational methods to design short (30 amino acid) peptides that fold to well-formed structures and spontaneously self-assemble into regular lattices. Rather than modify natural molecules, we have designed such peptides (their sequences and structures) from scratch using mathematical and computational methods. The sequences fold to form helical tetramers, and these provide building blocks that subsequently self-assemble into well-defined lattices. We have shown that distinct lattices (square, rectangular, hexagonal) can be achieved by carefully designing just the amino acids presented on the exterior of the building block. Thus these building blocks are versatile, and different building block structures are not needed to achieve different predetermined lattice structures. The nanometer-scale structures form reversibly and reproducibly. The larger micron-scale structure of the assemblies can be controlled with temperature, pH, and chemical modification of the peptides. The materials assemblies are robust and can be completely dissolved at high temperature but reform at lower temperatures. This approach provides a new route to achieve advanced materials that are precisely ordered across many length scales by designing chemical structure and processing conditions. These findings require the close integration of researchers with complementary expertise in theoretical chemistry, peptide synthesis, and nanostructure characterization.
Broader Impact: During the course of the project, students and postdoctoral researchers acquired skills and expertise associated with the next generation materials workforce. Students developed and shared complementary expertise: theory and computation; chemical and materials synthesis; manipulation and processing of materials and nanostructures; and measurement and characterization of materials across many length scales, from the atomic to the macroscopic. In collaboration with English, journalism, and writing programs, the team explored ways to enhance scientific communication and writing as well as the teaching of these important skills. The outreach work of the team involved sharing time, work and knowledge with students and teachers at K-12 schools and at higher education institutions serving students from groups that are underrepresented in science and engineering.
Last Modified: 01/03/2017
Modified by: Jeffery G Saven
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