IMMUNOCHEMICAL STUDIES ON TOBACCO MOSAIC VIRUS PROTEIN .7. BINDING OF OCTANOYLATED PEPTIDES OF TOBACCO MOSAIC VIRUS PROTEIN WITH ANTIBODIES TO WHOLE PROTEIN

It has been previously shown that a penta-peptide having the sequence Leu-Asp-Ala-Thr-Arg, representing residues 108-112 of the tobacco mosaic virus protein (TMVP), exhibited specific immunological binding with antibodies to the whole protein, whereas shorter C-terminal portions of this peptide did not. Subsequent experiments performed in this laboratory indicated that hydrophobicity of the N-terminal portion of the peptide may enhance binding with antibodies. The present communication reports on the synthesis of N-[14C]octanoyl derivatives of the C-terminal tetra-, tri-, and dipeptides of the above penta-peptide and on their capacity to bind with anti-TMVP and with antiacetylcholinesterase globulins. Results showed that the octanoyl-Asp-Ala-Thr-Arg and octanoyl-Ala-Thr-Arg exhibited specific binding with anti-TMVP whereas octanoyl-Thr-Arg did not. © 1968, American Chemical Society. All rights reserved.