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A Classical Synthesis of the Collagen‐like Peptides with the Sequence Z(GlyProPro) n OBu t and their characterization with circular dichroism and ultracentrifugation
Author(s) -
Bruckner Peter,
Rutschmann Beatrice,
Engel Jürgen,
Rothe Manfred
Publication year - 1975
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19750580506
Subject(s) - chemistry , circular dichroism , random coil , sequence (biology) , crystallography , helix (gastropod) , ultracentrifuge , triple helix , phase (matter) , stereochemistry , organic chemistry , chromatography , biochemistry , snail , biology , ecology
Abstract Oligopeptides with the sequence Z(GlyProPro) n OBu t (n = 3–7) were synthesized along a clasical pathway. Generally long fragments were condensed in order to allow an easy separation of the products from the reactants. It is established by molecular weight determination and measurements of circular dichroism that the peptides form the collagen‐like triple helix in methanol and that they assume the random coil conformation in dilute acetic acid. The circular dichroism spectra agree reasonably well with the corresponding spectra for (ProProGly) 10 which was obtained by solid phase synthesis in another laboratory.