Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1939103 | Biochemical and Biophysical Research Communications | 2006 | 5 Pages |
Abstract
Inhibitory peptide of papain-like cysteine proteases, affinity selected from a random disulfide constrained phage-displayed peptide library, was grafted to staphylococcal protein A’s B domain. Scaffold protein was additionally modified in order to allow solvent exposed display of peptide loop. Correct folding of fusion proteins was confirmed by CD-spectroscopy and by the ability to bind the Fc-region of rabbit IgG, a characteristic of parent domain. The recombinant constructs inhibited cathepsin L with inhibitory constants in the low-micromolar range.
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Authors
Tomaž Bratkovič, Aleš Berlec, Tatjana Popovič, Mojca Lunder, Samo Kreft, Uroš Urleb, Borut Štrukelj,