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Role of Engineered Proteins as Therapeutic Formulations
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Khushboo Gulati, Krishna Mohan Poluri
Kunitz domain is found in numerous proteases, including bovine pancreatic trypsin inhibitor (BPTI), human pancreatic secretory trypsin inhibitor (PSTI), and ecotin (periplasmic E. coli protease inhibitor). Kunitz domains are also involved as ion channel blockers as they mainly inhibit serine proteases. Structurally, kunitz domains are 60 amino acids long that are arranged in form of a mixture of α-helices and β-sheets. The core structure of the Kunitz domain is stabilized by three disulfide bonds that also make the structure compact and protect it from proteases (Ranasinghe and McManus, 2013). Lehmann et al. engineered small protein known as Ecallantide (DX-88) based on Kunitz domain using phage display technology. It acts as an inhibitor of plasma kallikrein that plays a major role in contact cascade to produce bradykinin (Lehmann, 2008). Dennis et al. designed Kunitz domain variants from Alzheimer’s amyloid beta-protein precursor inhibitor (APPI), to inhibit the association of human tissue factor-Factor VIIa complex (TF.FVIIa) (Dennis and Lazarus, 1994).
A comprehensive proteomics analysis of the response of Pseudomonas aeruginosa to nanoceria cytotoxicity
Published in Nanotoxicology, 2023
Lidija Izrael Živković, Nico Hüttmann, Vanessa Susevski, Ana Medić, Vladimir Beškoski, Maxim V. Berezovski, Zoran Minić, Ljiljana Živković, Ivanka Karadžić
Glycine betaine-binding protein, responsible for transporting glycine betaine, is osmotically dependent, and therefore, the downregulation implies a decrease of osmotic pressure, associated with cell extension noticed by TEM (Pulido-Reyes et al. 2015; Alpaslan et al. 2017). Downregulation of ecotin, the serine protease inhibitor bound to the matrix exopolysaccharide of biofilm, implies changes not only on the surface at the single cell level, but also in the bacterial community. Downregulation of Skp-like protein and chaperone-SurA, both involved in the correct folding and assembly of outer membrane proteins, suggests a disordered outer membrane-bound periplasmic space.