Literature DB >> 20408722

Interfacial rheological properties of recombinant spider-silk proteins.

Cyrille Vézy1, Kevin D Hermanson, Thomas Scheibel, Andreas R Bausch.   

Abstract

Freestanding protein films are interesting for many applications ranging from microencapsulation to tissue engineering. Here, the authors use interfacial rheology to characterize the adsorption kinetics and the rheology of spider-silk films formed at an oil water interface. The high surface activity of the engineered spider-silk proteins results in a fast formation of highly stable films, which can be modified by the addition of phosphate ions to the solution.

Entities:  

Year:  2009        PMID: 20408722     DOI: 10.1116/1.3174930

Source DB:  PubMed          Journal:  Biointerphases        ISSN: 1559-4106            Impact factor:   2.456


  1 in total

1.  A conserved spider silk domain acts as a molecular switch that controls fibre assembly.

Authors:  Franz Hagn; Lukas Eisoldt; John G Hardy; Charlotte Vendrely; Murray Coles; Thomas Scheibel; Horst Kessler
Journal:  Nature       Date:  2010-05-13       Impact factor: 49.962

  1 in total

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