Rapid preparation of stable isotope labeled peptides that bind to target proteins by a phage library system

J Biomol NMR. 2006 Jan;34(1):23-30. doi: 10.1007/s10858-005-5054-0.


We have developed a system for directly isolating foreign peptides displayed on the N-terminus of the major coat protein of bacteriophage M13. The phage particle in this system is formed as a mixture of wild type and modified coat proteins. The N-terminal segment of the modified coat protein was mutated for chemical cleavage, in order to obtain the displayed peptide from the major coat protein. Using 13C, 15N- labeled medium, we introduced stable isotopes, 13C and/or 15N, into the coat proteins. The NMR spectra for the cleaved peptides from the phage particles could be recorded within a few days after the selection of the phage clone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage M13 / chemistry
  • Bacteriophage M13 / genetics
  • Bacteriophage M13 / metabolism
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism
  • Carbon Isotopes / metabolism
  • Isotope Labeling / methods*
  • Molecular Sequence Data
  • Nitrogen Isotopes / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Library*
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / metabolism


  • Capsid Proteins
  • Carbon Isotopes
  • Nitrogen Isotopes
  • Peptide Library
  • Peptides