Dephosphorylation of d-Peptide Derivatives to Form Biofunctional, Supramolecular Nanofibers/Hydrogels and Their Potential Applications for Intracellular Imaging and Intratumoral Chemotherapy
Citations Over TimeTop 1% of 2013 papers
Abstract
D-Peptides, as the enantiomers of the naturally occurring L-peptides, usually resist endogenous proteases and are presumably insensitive to most enzymes. But, it is unclear whether or how a phosphatase catalyzes the dephosphorylation from D-peptides. In this work, we examine the formation of the nanofibers of D-peptides via enzymatic dephosphorylation. By comparing the enzymatic hydrogelation of L-peptide and D-peptide based hydrogelators, we find that the chirality of the precursors of the hydrogelators affects little on the enzymatic hydrogelation resulted from the removal of the phosphate group from a tyrosine phosphate residue. The attachment of a therapeutic agent (e.g., taxol) or a fluorophore (e.g., 4-nitro-2,1,3-benzoxadiazole) to the D-peptide based hydrogelators affords a new type of biostable or biocompatible hydrogelators, which may find applications in intratumoral chemotherapy or intracellular imaging, respectively. This work, as the first comprehensive and systematic study of the unexpected enzymatic dephosphorylation of D-peptides, illustrates a useful approach to generate supramolecular hydrogels that have both biostability and other desired functions.
Related Papers
- → The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle(1984)330 cited
- → Measuring the Activities of Two-Component Regulatory System Phosphatases(2018)3 cited
- → Dephosphorylation of Microtubule-Binding Sites at the Neurofilament-H Tail Domain by Alkaline, Acid, and Protein Phosphatases1(1993)29 cited
- → Okadaic Acid‐Induced Inhibition of B‐50 Dephosphorylation by Presynaptic Membrane‐Associated Protein Phosphatases(1991)19 cited
- → Dephosphorylation of the deinhibitor protein by the PCSH protein phosphatase(1985)10 cited