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A Facile Cyclization Method Improves Peptide Serum Stability and Confers Intrinsic Fluorescence.


ABSTRACT: Peptides are a growing class of macromolecules used in pharmaceutics. The path toward the clinical use of candidate peptides involves sequence optimization and cyclization for stability and affinity. For internalized peptides, tagging is also often required for intracellular trafficking studies, although fluorophore conjugation has an impact on peptide binding, permeability, and localization. Herein, a strategy based on cysteine arylation with tetrafluoroterephthalonitrile (4F-2CN), which simultaneously cyclizes peptides and imparts fluorescence, is reported. The 4F-2CN cyclization of an M2 macrophage-targeting peptide yields, in a single step, a peptide with improved serum stability, intrinsic fluorescence, and increased binding affinity. In a murine breast cancer model, it is demonstrated that the intrinsic fluorescence from the cyclized peptide is sufficient for monitoring biodistribution by whole-organ fluorescence imaging and cell internalization by flow cytometry.

SUBMITTER: Ngambenjawong C 

PROVIDER: S-EPMC5730504 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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A Facile Cyclization Method Improves Peptide Serum Stability and Confers Intrinsic Fluorescence.

Ngambenjawong Chayanon C   Gustafson Heather H HH   Sylvestre Meilyn M   Pun Suzie H SH  

Chembiochem : a European journal of chemical biology 20171107 24


Peptides are a growing class of macromolecules used in pharmaceutics. The path toward the clinical use of candidate peptides involves sequence optimization and cyclization for stability and affinity. For internalized peptides, tagging is also often required for intracellular trafficking studies, although fluorophore conjugation has an impact on peptide binding, permeability, and localization. Herein, a strategy based on cysteine arylation with tetrafluoroterephthalonitrile (4F-2CN), which simult  ...[more]

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