Jan 27, 2004

Independent folding and conformational changes of the barnase module in the VL-barnase immunofusion: calorimetric evidence

FEBS Letters
Yaroslav I TsybovskyS P Martsev


Although stability is critical for in vivo application of immunotoxins, a thermodynamic description of their folding/stability is still lacking. We applied differential scanning calorimetry (DSC) to RNase-based immunofusion comprising barnase, cytotoxic RNase from Bacillus amyloliquefaciens, fused to the light chain variable domain (VL) of anti-human ferritin antibody F11. By analyzing DSC curves recorded with or without preheating and addition of the barnase-stabilizing ligand guanosine 3'-monophosphate, we (i). assigned two well-resolved thermal transitions to the VL and barnase modules of VL-barnase, (ii). demonstrated independent folding of these two modules, and (iii). showed altered stability of the barnase module, which resulted from the dimeric state of VL-barnase.

  • References29
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Mentioned in this Paper

Bacterial Proteins
Alkalescens-Dispar Group
Chimeric Proteins, Recombinant
Bacillus amyloliquefaciens
Bacillus amyloliquefaciens ribonuclease
Alkaline Ribonuclease
Protein Conformation

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