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 446000
Title Disulfide bond-stabilized physical gels of an asymmetric collagen-inspired telechelic protein polymer
Author(s) Pham, T.H.T.; Skrzeszewska, P.J.; Werten, M.W.T.; Rombouts, W.H.; Cohen Stuart, M.A.; Wolf, F.A. de; Gucht, J. van der
Source Soft Matter 9 (2013). - ISSN 1744-683X - p. 6391 - 6397.
DOI http://dx.doi.org/10.1039/c3sm50641j
Department(s) Physical Chemistry and Colloid Science
FBR Bioconversion
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2013
Abstract We designed and produced an asymmetric collagen-inspired telechelic protein polymer with end blocks that can form triple helices of different thermal stabilities. Both end blocks consist of a motif that can form triple helices at low temperature, but one of these blocks carries an additional cysteine residue at the end. The cysteine residues can form disulfide bridges under oxidizing conditions, leading to dimer formation. This effectively stabilizes the triple helices, resulting in a double melting peak in differential scanning calorimetry: one corresponding to helices without disulfide bridges and one at significantly higher temperature, corresponding to stabilized helices. Under reducing conditions, the disulfide bridges are broken and the molecule behaves similarly to the symmetric variant. We find that these disulfide bridges also lead to an increase of the elastic modulus of the helical polymer network, probably because the number of helices in the system increases and also the disulfide bridges can crosslink different triple helical nodes.
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