Structural changes of thin films from recombinant spider silk proteins upon post-treatment

E. Metwalli; U. Slotta; Charles Darko; S. V. Roth; T. Scheibel; C. M. Papadakis

Structural changes of thin films from recombinant spider silk proteins upon post-treatment

E. Metwalli, U. Slotta, Charles Darko, S. V. Roth, T. Scheibel, C. M. Papadakis

Research output: Contribution to journal › Article › peer-review

Abstract

Engineering of spider silk proteins offers the possibility to control their molecular sequence and thus their material properties. Spin coating was used to prepare films of engineered spider silk protein derived from the garden spider’s ( Araneus diadematus ) dragline silk protein ADF-4. A conformational transition from α-helix to β-sheet-rich structures upon methanol treatment of the films was detected by external reflection IR spectroscopy. We present direct evidence for this structural transformation using grazing-incidence X-ray diffraction (GIXRD) and small-angle scattering (GISAXS). The protein film structure after the methanol treatment consists mainly of β-sheet polyalanine crystals dispersed in an amorphous protein matrix. The GIXRD intensity profiles show Bragg peaks from β-sheet polyalanine crystallites having an average size of 7.5 nm. The non-uniform and large crystal size distributions within the film were explained based on the protein composition. The effect of the chemical nature of the interface on the protein film structure was investigated as well.

Original language	English
Pages (from-to)	655-661
Number of pages	7
Journal	Applied Physics A
Volume	89
Issue number	3
Publication status	Published - Nov 2007

Cite this

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title = "Structural changes of thin films from recombinant spider silk proteins upon post-treatment",

abstract = "Engineering of spider silk proteins offers the possibility to control their molecular sequence and thus their material properties. Spin coating was used to prepare films of engineered spider silk protein derived from the garden spider{\textquoteright}s ( Araneus diadematus ) dragline silk protein ADF-4. A conformational transition from α-helix to β-sheet-rich structures upon methanol treatment of the films was detected by external reflection IR spectroscopy. We present direct evidence for this structural transformation using grazing-incidence X-ray diffraction (GIXRD) and small-angle scattering (GISAXS). The protein film structure after the methanol treatment consists mainly of β-sheet polyalanine crystals dispersed in an amorphous protein matrix. The GIXRD intensity profiles show Bragg peaks from β-sheet polyalanine crystallites having an average size of 7.5 nm. The non-uniform and large crystal size distributions within the film were explained based on the protein composition. The effect of the chemical nature of the interface on the protein film structure was investigated as well.",

author = "E. Metwalli and U. Slotta and Charles Darko and Roth, {S. V.} and T. Scheibel and Papadakis, {C. M.}",

year = "2007",

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T1 - Structural changes of thin films from recombinant spider silk proteins upon post-treatment

AU - Metwalli, E.

AU - Slotta, U.

AU - Darko, Charles

AU - Roth, S. V.

AU - Scheibel, T.

AU - Papadakis, C. M.

PY - 2007/11

Y1 - 2007/11

N2 - Engineering of spider silk proteins offers the possibility to control their molecular sequence and thus their material properties. Spin coating was used to prepare films of engineered spider silk protein derived from the garden spider’s ( Araneus diadematus ) dragline silk protein ADF-4. A conformational transition from α-helix to β-sheet-rich structures upon methanol treatment of the films was detected by external reflection IR spectroscopy. We present direct evidence for this structural transformation using grazing-incidence X-ray diffraction (GIXRD) and small-angle scattering (GISAXS). The protein film structure after the methanol treatment consists mainly of β-sheet polyalanine crystals dispersed in an amorphous protein matrix. The GIXRD intensity profiles show Bragg peaks from β-sheet polyalanine crystallites having an average size of 7.5 nm. The non-uniform and large crystal size distributions within the film were explained based on the protein composition. The effect of the chemical nature of the interface on the protein film structure was investigated as well.

AB - Engineering of spider silk proteins offers the possibility to control their molecular sequence and thus their material properties. Spin coating was used to prepare films of engineered spider silk protein derived from the garden spider’s ( Araneus diadematus ) dragline silk protein ADF-4. A conformational transition from α-helix to β-sheet-rich structures upon methanol treatment of the films was detected by external reflection IR spectroscopy. We present direct evidence for this structural transformation using grazing-incidence X-ray diffraction (GIXRD) and small-angle scattering (GISAXS). The protein film structure after the methanol treatment consists mainly of β-sheet polyalanine crystals dispersed in an amorphous protein matrix. The GIXRD intensity profiles show Bragg peaks from β-sheet polyalanine crystallites having an average size of 7.5 nm. The non-uniform and large crystal size distributions within the film were explained based on the protein composition. The effect of the chemical nature of the interface on the protein film structure was investigated as well.

M3 - Article

SN - 0947-8396

VL - 89

SP - 655

EP - 661

JO - Applied Physics A

JF - Applied Physics A

IS - 3

ER -

Structural changes of thin films from recombinant spider silk proteins upon post-treatment

Abstract

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