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.

Agency
National Science Foundation (NSF)
Institute
Division of Molecular and Cellular Biosciences (MCB)
Type
Standard Grant (Standard)
Application #
1243656
Program Officer
Wilson Francisco
Project Start
Project End
Budget Start
2013-08-01
Budget End
2018-06-30
Support Year
Fiscal Year
2012
Total Cost
$492,459
Indirect Cost
Name
Haverford College
Department
Type
DUNS #
City
Haverford
State
PA
Country
United States
Zip Code
19041