Engineered staphylococcal protein A's IgG-binding domain with cathepsin L inhibitory activity

Journal Article · Fri Oct 13 00:00:00 EDT 2006 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2006.08.078· OSTI ID:20854519

Bratkovic, Tomaz ^[1]; Berlec, Ales ^[2]; Popovic, Tatjana ^[2]; Lunder, Mojca ^[3]; Kreft, Samo ^[3]; Urleb, Uros ^[4]; Strukelj, Borut ^[3]

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1. Faculty of Pharmacy, Department of Pharmaceutical Biology, University of Ljubljana, Askerceva 7, SI-1000 Ljubljana (Slovenia) and Lek Pharmaceuticals, Drug Discovery, Verovskova 57, SI-1526 Ljubljana (Slovenia)
2. Jozef Stefan Institute, Department of Biochemistry and Molecular Biology, Jamova 39, SI-1000 Ljubljana (Slovenia)
3. Faculty of Pharmacy, Department of Pharmaceutical Biology, University of Ljubljana, Askerceva 7, SI-1000 Ljubljana (Slovenia)
4. Lek Pharmaceuticals, Drug Discovery, Verovskova 57, SI-1526 Ljubljana (Slovenia)

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.

• OSTI ID: 20854519
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 349; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AFFINITY
BACTERIOPHAGES
CATHEPSINS
CYSTEINE
DISULFIDES
PAPAIN
PEPTIDES
RABBITS
SPECTROSCOPY
STAPHYLOCOCCUS