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Peptide Synthesis

  • Brian Austen
Part of the Methods in Molecular Biology™ book series (MIMB, volume 3)

Abstract

Peptides are required for many different aspects of biotechnology. Since DNA sequences are generally functional only in the protein for which they code, the explosion in sequences that are known has led to an increase in the requirement for synthetic peptides. Quite often, the peptide will be haptenized to a protein carrier and then used to raise antibodies that will then recognize the parent protein. In other instances, synthetic peptides with biological activity will be required in high purity for testing in functional assays. The synthesis of peptide analogs that differ from the naturally occurring sequence in key residues are also often in demand. The methods described here are suitable for making peptides up to about 20 residues in length and do not require sophisticated equipment or highly toxic chemicals such as hydrogen fluoride.

Keywords

Molar Excess Mercuric Acetate Ninhydrin Reagent Fume Cupboard Fivefold Excess 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Barany, G. and Merrifield, R. B. (1980) Solid-phase Peptide Synthesis, in The Pep tides vol. 2 (Gross, E. and Meienhofer, J., eds) Academic, New York.Google Scholar
  2. 2.
    Meienhofer, J., Waki, M., Heimer, E. P., Lambros, T. J., Makofske, R. C., and Chang, C.-D. (1979) Solid-phase synthesis without repetitive acidolysis. Int. J. Peptide Protein Res. 13, 35–42.CrossRefGoogle Scholar
  3. 3.
    Arshady, R., Atherton, E., Gait, M. J., Lee, K., and Sheppard, R. C. (1979) Easily prepared polar support for solid phase peptide and oligonucleotide synthesis. Preparation of Substance P and a nonadeoxyribonucleotide. J. Chem. Soc. Chem. Commun. 423–425.Google Scholar
  4. 4.
    Carpino, L. A. and Han, G. Y. (1972) The 9-fluoren-ylmethoxycarbonyl amino-protecting group. J. Org. Chem. 37, 3404–3409.CrossRefGoogle Scholar
  5. 5.
    Kent, S. B. H. (1985) Difficult Sequences in Stepwise Peptide Synthesis; Common Molecular Origins in Solution and Solid Phase, in Peptid.es; Structure and Function Proc. 9th American Peptide Symposium. (Deber, C. M., Hruby, V. J., and Kopple, K. D., eds.) Pierce Chemical Co., Toronto, Ontario.Google Scholar
  6. 6.
    Wang, S.-S. (1973) p-Alkoxybenzyl alcohol resin and p-alkoxybenzyloxcarbonylhydrazide resin for solid-phase synthesis of protected peptide fragments. J. Am. Chem. Soc. 95, 1328–1333.PubMedGoogle Scholar
  7. 7.
    Paquet, A. (1981) Introduction of protecting groups into O-unprotected hydroxyamino acids using succinimidyl carbonates. Can]. Chem. 60, 976–980.CrossRefGoogle Scholar
  8. 8.
    Green, N., Alexander, H., Olson, A., Alexander, S., Shinnick, T. M., Sutcliffe, J. G., and Lemer, R. A. (1982) Immunogenic structure of the influenza virus hemagglutinin. Cell 28, 477–484.PubMedCrossRefGoogle Scholar
  9. 9.
    Sarin, V. K., Kent, S. B. H., Tarn, J. P., and Merrifield, R. B. (1981) Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reagent. Anal. Biochem. 117, 147–157.PubMedCrossRefGoogle Scholar

Copyright information

© The Humana Press Inc. 1988

Authors and Affiliations

  • Brian Austen
    • 1
  1. 1.Peptide Unit, Department of SurgerySt. George’s Medical SchoolLondonUK

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