Silk Modifications for Tunable Materials
Abstract
The objective of this renewal proposal is to gain fundamental insight into the role of tyrosines inthe control and modulation of silkworm silk self-assembly and the resulting materials properties.Silk is the model system for study due to our prior understanding of solution behavior and itsrole as a unique and highly versatile material with widespread applications in materials science,engineering, and biology. In our current project on stabilization of bioactive compounds in silk,we identified a key role of tyrosines as modulators of protein assembly, and in turn, materialproperties. We hypothesize that detailed examination of the role of tyrosines in silk selfassemblywill enable more tunable control of functional features of silk materials. Our goal is tofocus on methods to control and modify tyrosine interactions in silk and to study the impact onmaterial properties. To address these goals, two objectives will be pursued: (1) modulatingtyrosine crosslinks in order to control the degree of tyrosine-tyrosine covalent interactions, andto understand impact on structure-function and material properties. Both enzymatic andchemical crosslinking reactions will be pursued to modulate the rate and extent of dityrosinecrosslinks formed. (2) Chemical modifications of tyrosines to modulate self-assembly andcrystallization of silk. The objective is to utilize selective chemical modifications of the tyrosinesto systematically introduce new chemistries and evaluate the impact on secondary structure andultimately material properties. As a result of this work, we anticipate specific insight into thecentral role of tyrosines in modulating self-assembly of silk, as well as modes to further controlthe process via inhibiting or accelerating protein assembly. These insights have broaderimplications towards a wide range of biologically-derived materials, where tyrosines can beencoded (or are present naturally) as key biophysical
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Sep 11, 2017
- Source ID
- FA95501710333
Entities
People
- David L. Kaplan
Organizations
- Air Force Office of Scientific Research
- Tufts University
- United States Air Force