Integrin targeting fluorescent proteins: exploration of RGD insertion sites
Autor: | Jurgen Schill, MH Michael Sonntag, Luc Brunsveld |
---|---|
Přispěvatelé: | Chemical Biology |
Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Scaffold protein Integrins integrin Oligopeptides/chemistry Integrin protein-protein interactions Plasma protein binding Biochemistry Protein–protein interaction 03 medical and health sciences fluorescent probes Humans Fluorescent Dyes/chemistry Binding site Molecular Biology Peptide sequence Integrins/chemistry Fluorescent Dyes chemistry.chemical_classification RGD Binding Sites biology Chemistry Communication Organic Chemistry Genetic Variation protein engineering Protein engineering Molecular biology Communications Amino acid Cell biology 030104 developmental biology biology.protein Molecular Medicine Oligopeptides Protein Binding |
Zdroj: | Chembiochem ChemBioChem, 18(5). Wiley-VCH Verlag |
ISSN: | 1439-4227 |
Popis: | The potential of the fluorescent protein scaffold in controlling peptide sequence functionality is illustrated via the exploration of fluorescent proteins as novel probes for targeting of integrins. A library of fluorescent mCitrine proteins with RGD motifs incorporated at several positions in loops within the protein main chain was generated and characterized. Amino acid mutations to RGD as well as RGD motif insertions were evaluated and both approaches led to mCitrine constructs with typical fluorescent properties. Screening experiments against four human integrin receptors revealed two strong binding constructs and two selective integrin binders. The importance of the site of RGD incorporation illustrates the effect of the protein scaffold on RGD sequence functionality, leading to fluorescent protein constructs with the potential for selective integrin targeting. |
Databáze: | OpenAIRE |
Externí odkaz: |