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Molecular engineering of avidin and hydrophobin for functional self-assembling interfaces

Research output: Contribution to journalArticleScientificpeer-review


Original languageEnglish
Pages (from-to)102-109
Number of pages8
JournalColloids and Surfaces B: Biointerfaces
Publication statusPublished - 1 Aug 2014
Publication typeA1 Journal article-refereed


Control over the functionality of interfaces through biomolecular engineering is a central tool for nanoscale technology as well as many current applications of biology. In this work we designed fusion proteins that combined the surface adhesion and interfacial activity of a hydrophobin-protein together with the high affinity biotin-binding capability of an avidin-protein. We found that an overall architecture that was based on a circularly permuted version of avidin, dual-chain avidin, and hydrophobin gave a highly functional combination. The protein was produced in the filamentous fungus Trichoderma reesei and was efficiently purified using an aqueous two-phase partitioning procedure. The surface adhesive properties were widely different compared to wild-type avidin. Functional characterization showed that the protein assembled on hydrophobic surfaces as a thin layer even at very low concentrations and efficiently bound a biotinylated compound. The work shows how the challenge of creating a fusion protein with proteins that form multimers can be solved by structural design and how protein self-assembly can be used to efficiently functionalize interfaces.


  • Avidin, Biofunctional surface, Hydrophobin, Nanomaterial, Protein engineering