2 research outputs found
Chemoselective Dual Labeling of Native and Recombinant Proteins
The
attachment of two different functionalities in a site-selective
fashion represents a great challenge in protein chemistry. We report
site specific dual functionalizations of peptides and proteins capitalizing
on reactivity differences of cysteines in their free (thiol) and protected,
oxidized (disulfide) forms. The dual functionalization of interleukin
2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion
applying maleimide and disulfide rebridging allyl-sulfone groups.
In order to ensure broader applicability of the functionalization
strategy, a novel, short peptide sequence that introduces a disulfide
bridge was designed and site-selective dual labeling in the presence
of biogenic groups was successfully demonstrated
Synthesis of Peptide-Functionalized Poly(bis-sulfone) Copolymers Regulating HIV‑1 Entry and Cancer Stem Cell Migration
Peptide–polymer
conjugates have been regarded as primary
stronghold in biohybrid nanomedicine, which has seen extensive development
due to its intrinsic property to provide complementary functions of
both the peptide material and the synthetic polymer platform. Here
we present an advanced macromolecular therapeutic that targets two
exclusive classes of important diseases (namely, the HIV and cancer)
that are implicated by extremely different causative agents. Using
a facile thiol-reactive monomer, the eventual polymer facilitates
multivalent conjugation of an endogenous peptide WSC02 that targets
the CXCR4 chemokine receptor. The biohybrid material demonstrated
both potent antiviral effects against HIV-1 as well as inhibiting
cancer stem cell migration thus establishing the foundation for multimodal
nanotherapeutics that simultaneously target more than one class of
disease implications