期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 24, 期 9, 页码 751-763出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzr019
关键词
circular dichroism; epitope recognition; peptide aptamer; scaffold protein; microarray
资金
- BBSRC [BB/F011296/1]
- Leukaemia Research Fund [7508]
- AstraZeneca
- Yorkshire Cancer Research [L346]
- EPSRC [EP/G061394/1]
- Biotechnology and Biological Sciences Research Council [BB/F011296/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/G061394/1] Funding Source: researchfish
- BBSRC [BB/F011296/1] Funding Source: UKRI
- EPSRC [EP/G061394/1] Funding Source: UKRI
Constrained binding peptides (peptide aptamers) may serve as tools to explore protein conformations and disrupt proteinprotein interactions. The quality of the protein scaffold, by which the binding peptide is constrained and presented, is of crucial importance. SQT (Stefin A Quadruple MutantTracy) is our most recent development in the Stefin A-derived scaffold series. Stefin A naturally uses three surfaces to interact with its targets. SQT tolerates peptide insertions at all three positions. Peptide aptamers in the SQT scaffold can be expressed in bacterial, yeast and human cells, and displayed as a fusion to truncated pIII on phage. Peptides that bind to CDK2 can show improved binding in protein microarrays when presented by the SQT scaffold. Yeast two-hybrid libraries have been screened for binders to the POZ domain of BCL-6 and to a peptide derived from PBP2', specific to methicillin-resistant Staphylococcus aureus. Presentation of the Noxa BH3 helix by SQT allows specific interaction with Mcl-1 in human cells. Together, our results show that Stefin A-derived scaffolds, including SQT, can be used for a variety of applications in cellular and molecular biology. We will henceforth refer to Stefin A-derived engineered proteins as Scannins.
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