Beating the Heat - Fast Scanning Melts Silk Beta Sheet Crystals

被引:156
作者
Cebe, Peggy [1 ]
Hu, Xiao [2 ]
Kaplan, David L. [2 ]
Zhuravlev, Evgeny [3 ]
Wurm, Andreas [3 ]
Arbeiter, Daniela [3 ]
Schick, Christoph [3 ]
机构
[1] Tufts Univ, Dept Phys & Astron, Medford, MA 02155 USA
[2] Tufts Univ, Dept Biomed Engn, Medford, MA 02155 USA
[3] Univ Rostock, Inst Phys, D-18051 Rostock, Germany
基金
美国国家科学基金会;
关键词
THERMAL-ANALYSIS; WATER; PROTEINS; SPECTROSCOPY; RELAXATION; CAPACITY;
D O I
10.1038/srep01130
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];
摘要
Beta-pleated-sheet crystals are among the most stable of protein secondary structures, and are responsible for the remarkable physical properties of many fibrous proteins, such as silk, or proteins forming plaques as in Alzheimer's disease. Previous thinking, and the accepted paradigm, was that beta-pleated-sheet crystals in the dry solid state were so stable they would not melt upon input of heat energy alone. Here we overturn that assumption and demonstrate that beta-pleated-sheet crystals melt directly from the solid state to become random coils, helices, and turns. We use fast scanning chip calorimetry at 2,000 K/s and report the first reversible thermal melting of protein beta-pleated-sheet crystals, exemplified by silk fibroin. The similarity between thermal melting behavior of lamellar crystals of synthetic polymers and beta-pleated-sheet crystals is confirmed. Significance for controlling beta-pleated-sheet content during thermal processing of biomaterials, as well as towards disease therapies, is envisioned based on these new findings.
引用
收藏
页数:7
相关论文
共 38 条
[1]
Scanning microcalorimetry at high cooling rate [J].
Adamovsky, SA ;
Minakov, AA ;
Schick, C .
THERMOCHIMICA ACTA, 2003, 403 (01) :55-63
[2]
1,000,000-DEGREES-C/S THIN-FILM ELECTRICAL HEATER - IN-SITU RESISTIVITY MEASUREMENTS OF AL AND TI/SI THIN-FILMS DURING ULTRA-RAPID THERMAL ANNEALING [J].
ALLEN, LH ;
RAMANATH, G ;
LAI, SL ;
MA, Z ;
LEE, S ;
ALLMAN, DDJ ;
FUCHS, KP .
APPLIED PHYSICS LETTERS, 1994, 64 (04) :417-419
[3]
Silk-based biomaterials [J].
Altman, GH ;
Diaz, F ;
Jakuba, C ;
Calabro, T ;
Horan, RL ;
Chen, JS ;
Lu, H ;
Richmond, J ;
Kaplan, DL .
BIOMATERIALS, 2003, 24 (03) :401-416
[4]
Self-assembly of spider silk proteins is controlled by a pH-sensitive relay [J].
Askarieh, Glareh ;
Hedhammar, My ;
Nordling, Kerstin ;
Saenz, Alejandra ;
Casals, Cristina ;
Rising, Anna ;
Johansson, Jan ;
Knight, Stefan D. .
NATURE, 2010, 465 (7295) :236-U125
[5]
What vibrations tell us about proteins [J].
Barth, A ;
Zscherp, C .
QUARTERLY REVIEWS OF BIOPHYSICS, 2002, 35 (04) :369-430
[6]
The infrared absorption of amino acid side chains [J].
Barth, A .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2000, 74 (3-5) :141-173
[7]
CRYSTALLIZATION BEHAVIOR OF POLY(ETHERETHERKETONE) [J].
CEBE, P ;
HONG, SD .
POLYMER, 1986, 27 (08) :1183-1192
[8]
Ultrasensitive, fast, thin-film differential scanning calorimeter [J].
Efremov, MY ;
Olson, EA ;
Zhang, M ;
Schiettekatte, F ;
Zhang, ZS ;
Allen, LH .
REVIEW OF SCIENTIFIC INSTRUMENTS, 2004, 75 (01) :179-191
[9]
SECONDARY STRUCTURE AND DOSAGE OF SOLUBLE AND MEMBRANE-PROTEINS BY ATTENUATED TOTAL REFLECTION FOURIER-TRANSFORM INFRARED-SPECTROSCOPY ON HYDRATED FILMS [J].
GOORMAGHTIGH, E ;
CABIAUX, V ;
RUYSSCHAERT, JM .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1990, 193 (02) :409-420
[10]
A conserved spider silk domain acts as a molecular switch that controls fibre assembly [J].
Hagn, Franz ;
Eisoldt, Lukas ;
Hardy, John G. ;
Vendrely, Charlotte ;
Coles, Murray ;
Scheibel, Thomas ;
Kessler, Horst .
NATURE, 2010, 465 (7295) :239-U131