Better explicating the strengths and shortcomings of these models will help refine projections and improve transparency in the years ahead.
Image credit: Witsawat.S.
Contributed by Peter G. Schultz
Abstract
An antibody generated to an α-keto amide containing hapten 1 catalyzes the cis-trans isomerization of peptidyl-prolyl amide bonds in peptides and in the protein RNase T1. The antibody-catalyzed peptide isomerization reaction showed saturation kinetics for the cis-substrate, Suc-Ala-Ala-Pro-Phe-pNA, with a kcat/Km value of 883 s−1⋅M−1; the reaction was inhibited by the hapten analog 13 (Ki = 3.0 ± 0.4 μM). Refolding of denatured RNase T1 to its native conformation also was catalyzed by the antibody, with the antibody-catalyzed folding reaction inhibitable both by the hapten 1 and hapten analog 13. These results demonstrate that antibodies can catalyze conformational changes in protein structure, a transformation involved in many cellular processes.
Footnotes
ABBREVIATIONS
- FKBP,
- FK506/rapamycin-binding proteins;
- THF,
- tetrahydrofuran;
- HOBT,
- 1-hydroxybenzotriazole hydrate;
- DMF,
- dimethylformamide;
- EDC,
- 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride;
- TFA,
- trifluoroacetic acid;
- DIEA,
- diisopropylethylamine;
- DMSO,
- dimethyl sulfoxide;
- TFE,
- trifluoroethanol
- Accepted April 22, 1998.
- Copyright © 1998, The National Academy of Sciences
Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1
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