ArticleProtein engineering, design & selection : PEDS2010
Structure-function studies of an engineered scaffold protein derived from stefin A. I: Development of the SQM variant.
Article in Protein engineering, design & selection : PEDS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Structural Transition-Induced Raman Enhancement in Bioinspired Diphenylalanine Peptide Nanotubes.ACS applied materials & interfaces · 2022Article
- Article
- Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.International journal of molecular sciences · 2021Review
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- Article
- Studies of the oligomerisation mechanism of a cystatin-based engineered protein scaffold.Scientific reports · 2019Article
- Superchiral Plasmonic Phase Sensitivity for Fingerprinting of Protein Interface Structure.ACS nano · 2017Article
- Alternative reagents to antibodies in imaging applications.Biophysical reviews · 2017Review
- Development of a multipurpose scaffold for the display of peptide loops.Protein engineering, design & selection : PEDS · 2017Article
- Non-antibody protein-based biosensors.Essays in biochemistry · 2016Review
- The use of a neutral peptide aptamer scaffold to anchor BH3 peptides constitutes a viable approach to studying their function.Cell death & disease · 2014Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
Non-antibody scaffold proteins are used for a range of applications, especially the assessment of protein-protein interactions within human cells. The search for a versatile, robust and biologically neutral scaffold previously led us to design STM (stefin A triple mutant), a scaffold derived from the intracellular protease inhibitor stefin A. Here, we describe five new STM-based scaffold proteins that contain modifications designed to further improve the versatility of our scaffold. In a step-by-step approach, we introduced restriction sites in the STM open reading frame that generated new peptide insertion sites in loop 1, loop 2 and the N-terminus of the scaffold protein. A second restriction site in 'loop 2' allows substitution of the native loop 2 sequence with alternative oligopeptides. None of the amino acid changes interfered significantly with the folding of the STM variants as assessed by circular dichroism spectroscopy. Of the five scaffold variants tested, one (stefin A quadruple mutant, SQM) was chosen as a versatile, stable scaffold. The insertion of epitope tags at varying positions showed that inserts into loop 1, attempted here for the first time, were generally well tolerated. However, N-terminal insertions of epitope tags in SQM had a detrimental effect on protein expression.
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