Titelangaben
Liebmann, Burkhard ; Hümmerich, Daniel ; Scheibel, Thomas ; Fehr, Marcus:
Formulation of poorly water-soluble substances using self-assembling spider silk protein.
In: Colloids and Surfaces A: Physicochemical and Engineering Aspects.
Bd. 331
(2008)
Heft 1-2
.
- S. 126-132.
ISSN 0927-7757
DOI: https://doi.org/10.1016/j.colsurfa.2008.04.005
Abstract
In nature self-assembly of soluble monomeric proteins to defined supramolecular structures is an essential
process in the formation of morphologically distinct biological materials like cells, tissues, diatoms or
mollusk shells. Using these proteins, complex structures in the nanometer and micrometer scale can be
generated that are hardly obtainable by other methods. The engineered ADF4(C16) spider silk protein
is mimicking the sequence of the dragline silk protein ADF4 of the spider Araneus diadematus and can
be synthesized by a biotechnological production process using Escherichia coli (E. coli) as host organism.
From the soluble ADF4(C16) monomers assembly of nanofibers, microbeads and films is possible. The
purified monomeric ADF4(C16) strongly interacts with hydrophobic surfaces and particles of poorlywatersoluble
substances. Based on this effect ADF4(C16) could be used for colloidal stabilization of hydrophobic
particles in aqueous environment. Poorlywater-soluble substances can also be encapsulated in ADF4(C16)
microbeads during self-assembly. The release of the encapsulated ingredientswas induced by proteolytic
cleavage of the microbead structure. These results show that ADF4(C16) protein microbeads have a high
potential as a storage and delivery systemfor poorlywater-soluble active ingredients in several application
fields like cosmetics, pharma or nutrition.