Abstract
The specific recognition of peptides, which we define to include unstructured regions or denatured forms of proteins, is an intrinsic part of a multitude of biochemical assays and procedures. Many cellular interactions are also based on this principle as well. While it would be highly desirable to have a stockpile of sequence-specific binders for essentially any sequence, a de novo selection of individual binders against every possible target peptide sequence would be rather difficult to reduce to practice. Modular peptide binders could overcome this problem, as preselected and/or predesigned modules could be reused for the generation of new binders and thereby revolutionize the generation of binding proteins. This minireview summarizes advances in the development of peptide binders and possible scaffolds for their design.
Funding: Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Grant/Award Number: CRSII3_141832, Sinergia Program).
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©2017 Walter de Gruyter GmbH, Berlin/Boston
Articles in the same Issue
- Frontmatter
- Guest Editorial
- Highlight issue: protein design
- HIGHLIGHT: MOSBACH COLLOQUIUM 2016 “PROTEIN DESIGN”
- Multifunctional biomaterial coatings: synthetic challenges and biological activity
- Advances in the design and engineering of peptide-binding repeat proteins
- Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones
- Anticalins directed against vascular endothelial growth factor receptor 3 (VEGFR-3) with picomolar affinities show potential for medical therapy and in vivo imaging
- Development of a screening system for inteins active in protein splicing based on intein insertion into the LacZα-peptide
- A FACS-based screening strategy to assess sequence-specific RNA-binding of Pumilio protein variants in E. coli
- Review
- Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications
- Research Articles/Short Communications
- Protein Structure and Function
- A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III
- Comparison of the ability of mammalian eEF1A1 and its oncogenic variant eEF1A2 to interact with actin and calmodulin
- Structural analysis and interaction studies of acyl-carrier protein (acpP) of Staphylococcus aureus, an extraordinarily thermally stable protein
- Characterization of a new toxin from the entomopathogenic fungus Metarhizium anisopliae: the ribotoxin anisoplin
Articles in the same Issue
- Frontmatter
- Guest Editorial
- Highlight issue: protein design
- HIGHLIGHT: MOSBACH COLLOQUIUM 2016 “PROTEIN DESIGN”
- Multifunctional biomaterial coatings: synthetic challenges and biological activity
- Advances in the design and engineering of peptide-binding repeat proteins
- Fusion proteins of an enoate reductase and a Baeyer-Villiger monooxygenase facilitate the synthesis of chiral lactones
- Anticalins directed against vascular endothelial growth factor receptor 3 (VEGFR-3) with picomolar affinities show potential for medical therapy and in vivo imaging
- Development of a screening system for inteins active in protein splicing based on intein insertion into the LacZα-peptide
- A FACS-based screening strategy to assess sequence-specific RNA-binding of Pumilio protein variants in E. coli
- Review
- Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications
- Research Articles/Short Communications
- Protein Structure and Function
- A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III
- Comparison of the ability of mammalian eEF1A1 and its oncogenic variant eEF1A2 to interact with actin and calmodulin
- Structural analysis and interaction studies of acyl-carrier protein (acpP) of Staphylococcus aureus, an extraordinarily thermally stable protein
- Characterization of a new toxin from the entomopathogenic fungus Metarhizium anisopliae: the ribotoxin anisoplin