Reversible Protein Conjugation on Live Cell Surfaces by Specific Recognition between Coiled-Coil Motifs of Natural Amino Acid Sequences

Biomacromolecules. 2020 Sep 14;21(9):3539-3546. doi: 10.1021/acs.biomac.0c00569. Epub 2020 Jul 30.

Abstract

In this study, we propose a reversible covalent conjugation method for peptides, proteins, and even live cells based on specific recognition between natural amino acid sequences. Two heptad sequences can specifically recognize each other and induce the formation of a disulfide bond between cysteine residues. We show the covalent bond formation and dissociation between peptides and proteins in cell-free conditions and on the surface of live cells. Because heptad sequences consist of natural amino acids, they are expressed in cells without additional preparation and can be used to selectively conjugate peptides, proteins, and cells.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acids
  • Cysteine*
  • Peptides*
  • Protein Domains

Substances

  • Amino Acids
  • Peptides
  • Cysteine