Production in Pichia pastoris of protein-based polymers with small heterodimer-forming blocks

N.E. Domeradzka, M.W.T. Werten, R.J. de Vries, F.A. de Wolf

Research output: Contribution to journalArticleAcademicpeer-review

5 Citations (Scopus)

Abstract

Some combinations of leucine zipper peptides are capable of forming a-helical heterodimeric coiled coils with very high affinity. These can be used as physical cross-linkers in the design of protein-based polymers that form supramolecular structures, for example hydrogels, upon mixing solutions containing the complementary blocks. Such two-component physical networks are of interest for many applications in biomedicine, pharmaceutics, and diagnostics. This article describes the efficient secretory production of A and B type leucine zipper peptides fused to protein-based polymers in Pichia pastoris. By adjusting the fermentation conditions, we were able to significantly reduce undesirable proteolytic degradation. The formation of A-B heterodimers in mixtures of the purified products was confirmed by size exclusion chromatography. Our results demonstrate that protein-based polymers incorporating functional heterodimer-forming blocks can be produced with P. pastoris in sufficient quantities for use in future supramolecular self-assembly studies and in various applications.
Original languageEnglish
Pages (from-to)953-960
JournalBiotechnology and Bioengineering
Volume113
Issue number5
DOIs
Publication statusPublished - 2016

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