THE SYNTHESIS AND CHARACTERIZATION OF THE AMINO-TERMINAL OCTAPEPTIDE OF MOUSE NERVE GROWTH FACTOR

The octapeptide, Ser-Ser-Thr-His-Pro-Val-Phe-His, corresponding to the first eight amino-terminal residues in the sequence of mouse nerve growth factor, has been synthesized by the manual solid-phase technique. After cleavage of the peptide material from the peptide-resin by HF, extensive purification produced the expected product in good yield (27% of potential starting sites; 58% of the released product). The peptide was characterized by chromatographic techniques, sequence analysis, enzymatic digestion, CD and ORD spectral analyses, and biological and pharmacological assays. Detailed analysis of the reaction by-products, isolated during the purification of the principal product, provided technical information regarding possible synthetic side reactions and further evidence for dynamic solvation of the polymer matrix as a dominant factor in solid phase synthesis.