期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 276, 期 3, 页码 899-904出版社
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2000.3588
关键词
affinity; beta-turn; Biacore; CD; elastin; folding; helix; Protein A; sulphate; water
Elastin polymer sequences derived from muscle exhibit temperature and salt-induced reversible contractions and expansions. A folded and contracted beta-turn helical elastin structure is stabilised by increased intramolecular hydrophobic interactions. We have generated a switchable binding protein by inserting a typical elastin turn sequence, GVPGVG, between the two IgG-binding helices of an engineered globular minidomain from Protein A. This mutant showed increased binding of IgG-molecules compared to the wild-type sequence in the presence of sodium sulphate, as measured by surface plasmon resonance spectroscopy. Analysis by circular dichroism revealed a salt-induced folding of the mutant minidomain to a native type I beta-turn, likely stabilised as a result of the two interacting dehydrated valines across the beta-turn. Since sodium sulphate can be successfully used to regulate the folding/unfolding or binding/dissociation of this minidomain, this suggests an alternative protein purification method. (C) 2000 Academic Press.
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