Abstract: The peptide P₂(VYMSPF) selected from the phage display peptide library is an antagonist of aFGF, but its mechanism of influence on aFGF signal transduction is not clear. We used the two-dimensional electrophoresis and mass spectrometry technique to study the NIH₃T3 cell cultured in the blank IMDM medium and the IMDM mediums containing peptide P₂, aFGF+heparin, aFGF+heparin+peptide P₂ respectively. We selected five protein spots with altered expression in the latter two samples to perform mass spectrometry analysis and database search. Among the identified proteins, expression of three proteins was evidently decreased, including the guanine nucleotide-binding protein, alpha-11 subunit involved in the interior cellular signal transduction and nuclear factor 1C-type involved in the transcription regulation. In summary, these proteins provided the experimental base and clue for further study of the inhibition effect of P₂ on aFGF signal transduction.

Key words: Fibroblast growth factor, Six peptide, Two-dimensional electrophoresis