Physical Properties of Polymorphic Yeast Prion Amyloid Fibers
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Amyloid fibers play important roles in many human diseases and natural biological processes and have immense potential as novel nanomaterials. We explore the physical properties of polymorphic amyloid fibers formed by yeast prion protein Sup35. Amyloid fibers that conferred distinct prion phenotypes ([PSI[superscript +]]), strong (S) versus weak (W) nonsense suppression, displayed different physical properties. Both S[PSI[superscript +]] and W[PSI[superscript +]] fibers contained structural inhomogeneities, specifically local regions of static curvature in S[PSI[superscript +]] fibers and kinks and self-cross-linking in W[PSI[superscript +]] fibers. Force-extension experiments with optical tweezers revealed persistence lengths of 1.5 μm and 3.3 μm and axial stiffness of 5600 pN and 9100 pN for S[PSI[superscript +]] and W[PSI[superscript +]] fibers, respectively. Thermal fluctuation analysis confirmed the twofold difference in persistence length between S[PSI[superscript +]] and W[PSI[superscript +]] fibers and revealed a torsional stiffness of kinks and cross-links of ~100–200 pN·nm/rad.
Date issued
2011-07Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of Mechanical Engineering; Whitehead Institute for Biomedical ResearchJournal
Biophysical Journal
Publisher
Elsevier
Citation
Castro, Carlos E., Jijun Dong, Mary C. Boyce, Susan Lindquist, and Matthew J. Lang. “Physical Properties of Polymorphic Yeast Prion Amyloid Fibers.” Biophysical Journal 101, no. 2 (July 2011): 439–448. © 2011 Biophysical Society
Version: Final published version
ISSN
00063495
1542-0086