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Selective modification of sulfamidate-containing peptides.

Nuria Mazo1, Claudio D Navo2, Jesús M Peregrina1

  • 1Departamento de Química, Universidad de La Rioja, Centro de Investigación en Síntesis Química, E-26006 Logroño, Spain.

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Hybrid peptides with activated N-terminal cyclic sulfamidates offer versatile electrophilic reactivity. This enables site-selective peptide modifications and late-stage functionalization with various probes and drugs.

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Area of Science:

  • Organic Chemistry
  • Peptide Chemistry
  • Chemical Biology

Background:

  • Peptide modification is crucial for developing new therapeutics and chemical probes.
  • Developing efficient and site-selective methods for peptide functionalization remains a challenge.

Purpose of the Study:

  • To develop a novel peptide scaffold for versatile and site-selective late-stage functionalization.
  • To demonstrate the utility of this scaffold for installing diverse functionalities, including probes and drugs.

Main Methods:

  • Synthesis of hybrid peptides featuring α-methylisoserine-derived cyclic sulfamidates.
  • Nucleophilic ring-opening reactions with fluorescent probes, thiocarbohydrates, and click chemistry tags.
  • Attachment of affinity tags (biotin) and cytotoxic drugs (chlorambucil) for controlled release.
  • Investigation of base-promoted intramolecular acyl group migration.

Main Results:

  • The cyclic sulfamidate scaffold provides rich electrophilic reactivity for site- and stereoselective modifications.
  • Successful late-stage functionalization of the peptide backbone with various nucleophiles.
  • Demonstrated pH-controlled release of N-terminal drugs and efficient intramolecular modification of side chains.

Conclusions:

  • Activated hybrid peptides offer a powerful platform for stereocontrolled peptide backbone and side chain modification.
  • This methodology facilitates the development of novel peptide-based therapeutics and imaging agents.