Beating the heat-fast scanning melts silk beta sheet crystals

Scientific Reports

Volumn 3, Issue , 2013, Pages

  Cebe, Peggy ^a   Hu, Xiao ^b,d   Kaplan, David L ^b   Zhuravlev, Evgeny ^c   Wurm, Andreas ^c   Arbeiter, Daniela ^c   Schick, Christoph ^c  

^a Department of Physics and Astronomy ^*  (United States)

^b Tufts University   (United States)

^c UNIVERSITY OF ROSTOCK   (Germany)

^d ROWAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FIBROIN; SILK;

ANIMAL; ARTICLE; BOMBYX; CHEMISTRY; CRYSTALLIZATION; DIFFERENTIAL SCANNING CALORIMETRY; METABOLISM; PHASE TRANSITION; PROTEIN SECONDARY STRUCTURE; TRANSITION TEMPERATURE;

ANIMALS; BOMBYX; CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLIZATION; FIBROINS; PHASE TRANSITION; PROTEIN STRUCTURE, SECONDARY; SILK; TRANSITION TEMPERATURE;

MLCS; MLOWN;

EID: 84873156002     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep01130     Document Type: Article

References (37)

1. Shao, Z.&Vollrath, F. Materials: Surprising strength of silkworm silk. Nature 418, 741-741 (2002).
2. Omenetto, F. G. & Kaplan, D. L. New opportunities for an ancient material. Science 329, 528-531 (2010).
3. Lee, S.-M. et al. Greatly increased toughness of infiltrated spider silk. Science 324, 488-492 (2009).
4. Holland, C., Vollrath, F., Ryan, A. J. & Mykhaylyk, O. O. Silk and synthetic polymers: reconciling 100 degrees of separation. Adv. Mater. 24, 105-109 (2012).
5. Altman, G. H. et al. Silk-based biomaterials. Biomater. 24, 401-416 (2003). (Pubitemid 35291198)
6. Rockwood, D. N. et al.Materials fabrication from Bombyx mori silk fibroin. Nat. Protocols 6, 1612-1631 (2011).
7. Hu, X. et al. Regulation of silk material structure by temperature-controlled water vapor annealing. Biomacromolecules 12, 1686-1696 (2011).
8. Pritchard, E. M. & Kaplan, D. L. Silk fibroin biomaterials for controlled release drug delivery. Expert Opinion on Drug Delivery 8, 797-811 (2011).
9. Kaplan, D. L. et al. Silk. 103-133, Protein-Based Materials, McGrath, K. & Kaplan, D., Eds. (Birkhauser, Boston 1997).
10. Vepari, C. & Kaplan, D. L. Silk as a biomaterial. Prog. in Polym. Sci. 32, 991-1007 (2007). (Pubitemid 47198292)
11. Jin, H.-J. & Kaplan, D. L. Mechanism of silk processing in insects and spiders. Nature 424, 1057-1061 (2003). (Pubitemid 37064306)
12. Zheng, Y. et al. Directional water collection on wetted spider silk. Nature 463, 640-643 (2010).
13. Askarieh, G. et al. Self-assembly of spider silk proteins is controlled by a pHsensitive relay. Nature 465, 236-238 (2010).
14. Hagn, F. et al. A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature 465, 239-242 (2010).
15. Xu, M. & Lewis, R. V. Structure of a protein superfiber: spider dragline silk. Proc. Natl. Acad. Sci. USA 87, 7120-7124 (1990).
16. Hu, X., Kaplan, D. & Cebe, P. Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules 39, 6161-6170 (2006). (Pubitemid 44412191)
17. Hu, X., Kaplan, D. & Cebe, P. Dynamic protein2water relationships during b-sheet formation. Macromolecules 41, 3939-3948 (2008).
18. Hu, X., Kaplan, D. & Cebe, P. Effect of water on the thermal properties of silk fibroin. Thermochim. Acta 461, 137-144 (2007). (Pubitemid 47187461)
19. Allen, L. H. et al. 1000 000 "C/S thin film electrical heater: in situ resistivity measurements of Al and Ti/Si thin films during ultra rapid thermal annealing. Appl. Phys. Lett. 64, 417-419 (1994).
20. Efremov, M. Y. et al. Ultrasensitive, fast, thin-film differential scanning calorimeter. Rev. Sci. Instrum. 75, 179-191 (2004).
21. Lopeandia, A. F., Valenzuela, J. & Rodŕguez-Viejo, J. Power compensated thin film calorimetry at fast heating rates. Sensors and Actuators A: Physical 143, 256-264 (2008). (Pubitemid 351451847)
22. Zhuravlev, E.&Schick, C. Fast scanning power compensated differential scanning nano-calorimeter: 1. The device. Thermochim. Acta 505, 1-13 (2010).
23. Zhuravlev, E.&Schick, C. Fast scanning power compensated differential scanning nano-calorimeter: 2. Heat capacity analysis. Thermochim. Acta 505, 14-21 (2010).
24. Minakov, A. A. & Schick, C. Ultrafast thermal processing and nanocalorimetry at heating and cooling rates up to 1 MK/s. Rev. Sci. Instr. 78, 073902-073910 (2007).
25. Adamovsky, S. A.,Minakov,A. A.&Schick, C. Scanning microcalorimetry at high cooling rate. Thermochim. Acta 403, 55-63 (2003).
26. Barth, A. The infrared absorption of amino acid side chains. Progr. in Biophysics and Molecular Biology 74, 141-173 (2000). (Pubitemid 32168153)
27. Barth, A. & Zscherp, C. What vibrations tell about proteins. Quarterly Rev. of Biophysics 35, 369-430 (2002).
28. Cebe, P. & Hong, S. D. Crystallization behaviour of poly(ether-ether-ketone). Polymer 27, 1183-1192 (1986).
29. Minakov, A. A., Mordvintsev, D. A., Tol, R. & Schick, C. Melting and reorganization of the crystalline fraction and relaxation of the rigid amorphous fraction of isotactic polystyrene on fast heating (30,000 K/min). Thermochim. Acta 442, 25-30 (2006).
30. Warwicker, J. O. Comparative studies of fibroins: II. The crystal structures of various fibroins. J. of Molecular Biology 2, 350-362, IN351 (1960).
31. Pauling, L. & Corey, R. B. The pleated sheet, a new layer configuration of polypeptide chains. Proc. Natl. Acad. Sci. USA 37, 251-256 (1951).
32. Yu, L., Hu, X., Kaplan, D. & Cebe, P. Dielectric relaxation spectroscopy of hydrated and dehydrated silk fibroin cast from aqueous solution. Biomacromolecules 11, 2766-2775 (2010).
33. Hu, X., Kaplan, D., & Cebe, P. Thermal Analysis of Protein-Mettalic Ion Systems. J. Thermal Anal. Calorim. 96, 827-834 (2009).
34. van Herwaarden, A. W. Overview of calorimeter chips for various applications. Thermochim. Acta 432, 192-201 (2005). (Pubitemid 40785935)
35. Pyda, M.,Hu, X.&Cebe, P. Heat Capacity of Silk Fibroin Based on theVibrational Motion of Poly(amino acid)s in the Presence and Absence of Water. Macromolecules 41, 4786-4793 (2008).
36. Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J.-M. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fouriertransform infrared spectroscopy on hydrated films. Europ. J. of Biochemistry 193, 409-420 (1990). (Pubitemid 20344915)
37. Jung, C. Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy. J. Molecular Recognition 13, 325-351 (2000).