Hostname: page-component-cd9895bd7-p9bg8 Total loading time: 0 Render date: 2024-12-29T09:58:45.440Z Has data issue: false hasContentIssue false
  • English
  • Français

Inelastic Neutron Scattering Studies of Natural Silkworm Proteins

Published online by Cambridge University Press:  30 June 2015

Christopher Alan Crain ,
Nicholas A. Strange  and
J. Z. Larese
Christopher Alan Crain
Affiliation:
University of Tennessee, Knoxville, Tennessee, United States
Nicholas A. Strange
Affiliation:
University of Tennessee, Knoxville, Tennessee, United States
J. Z. Larese
Affiliation:
University of Tennessee, Knoxville, Tennessee, United States
Get access

Abstract

Understanding the interaction of water with biological materials is of fundamental importance. One of main driving forces behind the renewed activity of biomimetic materials involves the dramatic physical properties that many of them exhibit. Two main factors that are critical for understanding silks: the nanoscale semi-crystalline folding structure, and the degree of hydration of the disordered fraction. We describe our investigation of the preparation, characterization and inelastic neutron scattering (INS) studies of the microscopic dynamics of natural Bombyx mori silk fibroin proteins derived from silkworm cocoons. An in situ quartz microbalance is used for monitoring/controlling the hydration and solvent levels of the proteins electrospun onto neutron sample holders. By employing these novel methods our INS investigation facilitated a snapshot of the microscopic silk protein dynamics heretofore not investigated or reported. Preliminary INS measurements illustrate the effect of water and methanol interaction on the dynamics of the fibroin β-pleated sheet component. Evidence of what appears to be a water component (intersheet) distinct from bulk water is clearly apparent in the INS spectrum when the dynamical response from the dry silk is subtracted away.

Keywords

biomaterialneutron scatteringadsorption
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1793: Symposium GG – Foundations of Bio/Nano Interfaces―Synthesis, Modeling, Design Principles and Applications , 2015 , pp. 41 - 46
Copyright
Copyright © Materials Research Society 2015 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Kaplan, D.; PNAS 109, 11981 (2012).Google Scholar
McGrath, K, Kaplan, D, editors. Protein- based materials Boston: Birkhauser, 1997.CrossRefGoogle Scholar
Chen, F., Porter, D. & Vollrath, F; 2010 Phys. Rev. E82, 041911–041917 Google Scholar
Porter, D. and Vollrath, F.; Adv. Mater. 2009, 21, 487–492.CrossRefGoogle Scholar
Arntzen, C. J.; Ritter, E. M., Encyclopedia of agricultural science. Academic Press: San Diego, 1994.Google Scholar
Pérez-Rigueiro, J.; Viney, C.; Llorca, J.; Elices, M., Journal of Applied Polymer Science 2000, 75 (10), 1270–1277.3.0.CO;2-C>CrossRefGoogle Scholar
Marsh, RE, Corey, RB, Pauling, L. Biochim Biophys Acta 1955;16:1–34.CrossRefGoogle Scholar
Lotz, B.; Colonna Cesari, F., Biochimie 1979, 61 (2), 205–214.CrossRefGoogle Scholar
Goupil-Lamy, A. V.; Smith, J. C.; Yunoki, J.; Parker, S. F.; Kataoka, M. J. Am. Chem. Soc. 1997, 119, 9268–9273.CrossRefGoogle Scholar
Ohgo, Kosuke, Zhao, Chenhua, Kobayashi, Mitsuhiro, Asakura, Tetsuo, POLYMER 44, 841(2003).CrossRefGoogle Scholar
Seeger, P. A., Daemen, L. L., Larese, J. Z., Nuclear Instruments and Methods in Physics Research A, 604, 719–728, (2009).CrossRefGoogle Scholar
Middendorf, H. D.; Hayward, R. L.; Parker, S. F.; Bradshaw, J.; Miller, A. Biophys. J. 1995, 69, 660–673.CrossRefGoogle Scholar
Ruffle, Stuart V., Michalarias, Ilias, Li, Ji-Chen, and Ford, Robert C.; J. Am. Chem. Soc. 124, 565–569 (2002).CrossRefGoogle Scholar