Abstract
Perfluorinated organic compounds (PFCs) are nontoxic, biocompatible, bioavailable, and bioorthogonal species which possess the unique ability to segregate away from both polar and nonpolar solvents producing a compact fluorophilic phase. Traditional techniques of fluorous chemical proteomics are generally applied to enrich biological samples in target protein(s) exploiting this property of PFCs to build fluorinated probes able to covalently bind to protein ensembles and being selectively extracted by fluorophilic solvents. Aiming at building a strategy able to avoid irreversible modification of the analyzed biosystem, a novel fully noncovalent probe is presented as an enabling tool for the recognition and isolation of biological protein(s). In our strategy, both the fluorophilic extraction and the biorecognition of a selected protein successfully occur via the establishment of reversible but selective interactions.
Highlights
Perfluorinated organic compounds (PFCs) are nontoxic, biocompatible, bioavailable, and bioorthogonal species which possess the unique ability to segregate away from both polar and nonpolar solvents producing a compact fluorophilic phase
Perfluorinated organic compounds (PFCs), characterized by the complete substitution of a CmHn framework with a CmFn chain, are nontoxic,[8,9] biocompatible, bioavailable, and bioorthogonal[10] species largely exploited in vivo as enabling tools for innovative supramolecular bioapplications.[11−14] As an example, PFCs offer the possibility of acquiring in vivo imaging data through the application of 19F-magnetic resonance spectroscopy (MRS) and 19F magnetic resonance imaging (MRI).[15−20]
Biotin/avidin- or streptavidinbased systems are noteworthy examples of this strategy in which fluorolabeled biotin interacts and “tags” protein via chemical reactions with the ε-amino group of lysine residues allowing the selective extraction and recognition of tagged proteins.[40−44] While the fluorophilic interactions involved in FSPE are, by definition, noncovalent, the mechanisms of action of the fluoro-labeled probes employed in “classical” fluorous proteomics are mainly based on the establishment of a strong covalent bond with their biomolecular target(s)
Summary
Ferrandi − Istituto di Chimica del Riconoscimento Molecolare - Consiglio Nazionale delle Ricerche, Milano, Italy. Fabiana Vallone − Ospedale San Raffaele, Milano, Italy Annapaola Andolfo − Ospedale San Raffaele, Milano, Italy.
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