title: Tailoring small proteins towards biomedical applications.
abstract: Over the last two decades proteins have become increasingly important in human therapy and diagnosis. Engineering therapeutic proteins through improving their biological activity and stability has been a major interest in our group. In this mini-review we summarize our research on three proteins with pharmaceutical potential - serine protease inhibitor from squash seeds (CMTI), bovine pancreatic trypsin inhibitor (BPTI), and human fibroblast growth factor 1 (FGF1). To improve the functional properties of these proteins we used multiple techniques such as homology approach, rational design, total chemical synthesis, site-directed mutagenesis and phage display. The physicochemical properties of the obtained protein variants were evaluated using protein crystallography, spectroscopic techniques, enzymatic assays, stability measurements as well as numerous biological tests.
authors: Department of Protein Engineering, University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland.
authors: Malgorzata
authors: M
authors: Zakrzewska
authors: Anna
authors: A
authors: Szlachcic
authors: Jacek
authors: J
authors: Otlewski
mesh_terms: D000818:Animals; D007611:Aprotinin / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D002417:Cattle; D028464:Cucurbita / Q000737:chemistry; D055808:Drug Discovery / Q000379:methods*; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D006801:Humans; D016297:Mutagenesis, Site-Directed; D015202:Protein Engineering / Q000379:methods*; D055550:Protein Stability; D012639:Seeds / Q000737:chemistry; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology
chemical_list: D015842:Serine Proteinase Inhibitors; D016220:Fibroblast Growth Factor 1; D007611:Aprotinin