Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 372787
Title Biosynthesis of an amphiphilic silk-like polymer
Author(s) Werten, M.W.T.; Moers, A.P.H.A.; Vong, T.H.; Zuilhof, H.; Hest, J.C.M. van; Wolf, F.A. de
Source Biomacromolecules 9 (2008)7. - ISSN 1525-7797 - p. 1705 - 1711.
DOI https://doi.org/10.1021/bm701111z
Department(s) AFSG Biobased Products
Laboratory for Organic Chemistry
Publication type Refereed Article in a scientific journal
Publication year 2008
Keyword(s) covalently attached monolayers - extremely mild attachment - pichia-pastoris - periodic polypeptides - recombinant protein - circular-dichroism - crystal-structure - fibrous proteins - quantitative ir - visible-light
Abstract An amphiphilic silk-like protein polymer was efficiently produced in the yeast Pichia pastoris. The secreted product was fully intact and was purified by solubilization in formic acid and subsequent precipitation of denatured host proteins upon dilution with water. In aqueous alkaline solution, the negatively charged acidic polymer assumed extended helical (silk III-like) and unordered conformations. Upon subsequent drying, it assumed a conformation rich in ß-turns. In water at low pH, the uncharged polymer aggregated and the solution became turbid. Concentrated solutions in 70% (v/v) formic acid slowly formed gels. Replacement of the formic acid¿water mixture with methanol and subsequent drying resulted in ß-sheets, which stacked into fibril-like structures. The novel polymer instantaneously lowered the air¿water interfacial tension under neutral to alkaline conditions and reversed the polarity of hydrophobic and hydrophilic solid surfaces upon adsorption.
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