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.
|Original language||English (US)|
|Number of pages||8|
|Journal||International Journal of Peptide and Protein Research|
|Publication status||Published - Sep 1974|
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