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Beating the heat--fast scanning melts silk beta sheet crystals
Peggy Cebe1, Xiao Hu, David L Kaplan
1Department of Physics and Astronomy, Tufts University, Medford MA 02155, USA. peggy.cebe@tufts.edu
Scientific Reports
|January 26, 2013
Summary
Beta-pleated-sheet crystals, common in silk and associated with Alzheimer's disease, were previously thought to be thermally stable. This study demonstrates their reversible melting into random coils, challenging existing protein science paradigms.
Area of Science:
- Protein structure and dynamics
- Biomaterials science
- Polymer physics
Background:
- Beta-pleated-sheet crystals are highly stable protein secondary structures.
- These structures are crucial in fibrous proteins like silk and implicated in diseases such as Alzheimer's.
- The prevailing view was that these crystals do not melt solely from heat input in a dry solid state.
Purpose of the Study:
- To investigate the thermal stability and melting behavior of beta-pleated-sheet crystals.
- To challenge the established paradigm regarding the thermal melting of these protein structures.
- To explore the implications for biomaterial processing and disease therapies.
Main Methods:
- Utilized fast scanning chip calorimetry at an ultra-high rate of 2,000 K/s.
- Investigated the thermal transitions of silk fibroin as a model system for beta-pleated-sheet crystals.
- Analyzed the reversibility of the melting process.
Main Results:
- Demonstrated the direct melting of beta-pleated-sheet crystals from the solid state into random coils, helices, and turns.
- Reported the first instance of reversible thermal melting for protein beta-pleated-sheet crystals.
- Confirmed similarities between the thermal melting of beta-pleated-sheet crystals and synthetic polymer lamellar crystals.
Conclusions:
- Beta-pleated-sheet crystals can undergo reversible thermal melting, overturning previous assumptions.
- Findings have significant implications for controlling protein structure during thermal processing of biomaterials.
- New insights may contribute to developing therapies for diseases associated with beta-pleated-sheet aggregation.
