Retention of bioactive ligand conformation in a gaseous protein-trisaccharide complex

J Am Chem Soc. 2002 Nov 27;124(47):13980-1. doi: 10.1021/ja0281380.

Abstract

Arrhenius parameters, obtained with the blackbody infrared radiative dissociation technique, are reported for the dissociation of gaseous protonated complexes of a single-chain variable fragment (scFv) of the monoclonal antibody Se155-4 with structurally constrained trisaccharide ligands that resemble the bioactive conformer. The similarity in the dissociation activation energies measured for the +10 charge-state complexes of the constrained ligands and the native trisaccharide is evidence that the bioactive conformation of the native ligand is retained in the gas phase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / chemistry
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Gases
  • Immunoglobulin Fragments / chemistry*
  • Kinetics
  • Molecular Sequence Data
  • Protein Conformation
  • Spectrometry, Mass, Electrospray Ionization
  • Static Electricity
  • Trisaccharides / chemistry*

Substances

  • Antibodies, Monoclonal
  • Gases
  • Immunoglobulin Fragments
  • Trisaccharides