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Study of a regular polypeptide isomorphous to collagen and containing the sequence glycyl-prolyl-hydroxyprolyl

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Summary

  1. 1.

    The synthesis is described of a polypeptide containing the sequence glycyl-prolyl-hydroxyprolyl, isomorphous to the pseudocrystalline portions of collagen.

  2. 2.

    The tetraethyl pyrophosphite method was found to be the best of the methods proposed up to now for the preparation of regular polypeptides from free peptides.

  3. 3.

    In the course of the preparation of polypeptides by the tetraethyl pyrophosphite method the partial blocking of amino groups with phosphorus compounds occurs.

  4. 4.

    The molecular weight of the synthetic polypeptide was determined by various methods; fractionation of the polypeptide with respect to molecular weights was carried out on Sephadex G-25.

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Additional information

In conclusion the authors thank V. A. Shpikiter for determining sedimentation coefficients in the ultracentrifuge, T. D. Kozarenko for carrying out the amino acid analysis of the polypeptide, and N. S. Andreeva and M. I. Millionova for taking and interpreting the x-ray photographs.

Translated from Izvestiya Akademii Nauk SSSR, Setiya Khimicheskaya, No. 6, pp. 1043–1049, June, 1964

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Shibnev, V.A., Debabov, V.G. Study of a regular polypeptide isomorphous to collagen and containing the sequence glycyl-prolyl-hydroxyprolyl. Russ Chem Bull 13, 969–974 (1964). https://doi.org/10.1007/BF01141649

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Keywords

  • Collagen
  • Peptide
  • Molecular Weight
  • Phosphorus
  • Fractionation