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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Indium mediated allylation in peptide and protein functionalization.

Jenefer Alam1, Thomas H Keller, Teck-Peng Loh

  • 1Division of Chemistry and Biological Chemistry, School of Physical and Mathematical Sciences, 1 Nanyang Walk, Block 5 Level 3, Nanyang Technological University, Singapore 637371, Singapore.

Chemical Communications (Cambridge, England)
|July 15, 2011
PubMed
Summary

Indium-mediated allylation enables site-selective modification of peptide and protein N-terminal aldehydes. This study demonstrates the first use of indium for C-C bond formation in protein labeling under mild, eco-friendly conditions.

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Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Site-selective functionalization is crucial for modifying peptides and proteins.
  • Traditional methods often require harsh conditions or lack specificity.
  • N-terminal aldehydes present a unique handle for bioconjugation.

Purpose of the Study:

  • To investigate the utility of indium-mediated allylation for protein labeling.
  • To establish mild and environmentally friendly conditions for C-C bond formation in biomolecules.
  • To demonstrate site-selective functionalization at the N-terminus of peptides and proteins.

Main Methods:

  • Utilizing indium (In) as a catalyst for allylation reactions.
  • Applying the method to N-terminal aldehydes of peptides and proteins.
  • Performing reactions under mild, aqueous, and room-temperature conditions.

Main Results:

  • Successful site-selective C-C bond formation at the N-terminus of peptides and proteins.
  • Demonstration of indium-mediated allylation as a robust protein labeling technique.
  • Confirmation of mild and environmentally friendly reaction conditions.

Conclusions:

  • Indium-mediated allylation offers a novel and efficient approach for protein labeling.
  • This method provides a greener alternative for bioconjugation and chemical biology studies.
  • The site-selectivity and mild conditions make it suitable for complex biological systems.