The synthesis and characterization of the amino terminal octapeptide of mouse nerve growth factor

R. Hogue Angeletti, R. A. Bradshaw, G. R. Marshall

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The octapeptide, Ser Ser Thr His Pro Val Phe His, corresponding to the first 8 amino terminal residues in the sequence of mouse nerve growth factor, was 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, circular dichroism and optical rotatory dispersion spectral analyses, and biological and pharmacological assays. Detailed analysis of the reaction byproducts, 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 languageEnglish (US)
Pages (from-to)321-328
Number of pages8
JournalInternational Journal of Peptide and Protein Research
Volume6
Issue number5
StatePublished - 1974
Externally publishedYes

Fingerprint

Nerve Growth Factor
Peptides
Purification
Optical Rotatory Dispersion
Solid-Phase Synthesis Techniques
Solvation
Dichroism
Circular Dichroism
Polymer matrix
Biological Assay
Sequence Analysis
Byproducts
Digestion
Assays
Polymers
Resins
Pharmacology

ASJC Scopus subject areas

  • Biochemistry

Cite this

The synthesis and characterization of the amino terminal octapeptide of mouse nerve growth factor. / Hogue Angeletti, R.; Bradshaw, R. A.; Marshall, G. R.

In: International Journal of Peptide and Protein Research, Vol. 6, No. 5, 1974, p. 321-328.

Research output: Contribution to journalArticle

Hogue Angeletti, R. ; Bradshaw, R. A. ; Marshall, G. R. / The synthesis and characterization of the amino terminal octapeptide of mouse nerve growth factor. In: International Journal of Peptide and Protein Research. 1974 ; Vol. 6, No. 5. pp. 321-328.
@article{31fd7beedb044640b5b97f58f22fed13,
title = "The synthesis and characterization of the amino terminal octapeptide of mouse nerve growth factor",
abstract = "The octapeptide, Ser Ser Thr His Pro Val Phe His, corresponding to the first 8 amino terminal residues in the sequence of mouse nerve growth factor, was 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, circular dichroism and optical rotatory dispersion spectral analyses, and biological and pharmacological assays. Detailed analysis of the reaction byproducts, 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.",
author = "{Hogue Angeletti}, R. and Bradshaw, {R. A.} and Marshall, {G. R.}",
year = "1974",
language = "English (US)",
volume = "6",
pages = "321--328",
journal = "International Journal of Peptide and Protein Research",
issn = "0367-8377",
publisher = "Wiley-Blackwell",
number = "5",

}

TY - JOUR

T1 - The synthesis and characterization of the amino terminal octapeptide of mouse nerve growth factor

AU - Hogue Angeletti, R.

AU - Bradshaw, R. A.

AU - Marshall, G. R.

PY - 1974

Y1 - 1974

N2 - The octapeptide, Ser Ser Thr His Pro Val Phe His, corresponding to the first 8 amino terminal residues in the sequence of mouse nerve growth factor, was 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, circular dichroism and optical rotatory dispersion spectral analyses, and biological and pharmacological assays. Detailed analysis of the reaction byproducts, 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.

AB - The octapeptide, Ser Ser Thr His Pro Val Phe His, corresponding to the first 8 amino terminal residues in the sequence of mouse nerve growth factor, was 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, circular dichroism and optical rotatory dispersion spectral analyses, and biological and pharmacological assays. Detailed analysis of the reaction byproducts, 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.

UR - http://www.scopus.com/inward/record.url?scp=0016242815&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016242815&partnerID=8YFLogxK

M3 - Article

C2 - 4430560

AN - SCOPUS:0016242815

VL - 6

SP - 321

EP - 328

JO - International Journal of Peptide and Protein Research

JF - International Journal of Peptide and Protein Research

SN - 0367-8377

IS - 5

ER -