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Die Synthese eines Tetracosapeptides mit der Aminosäuresequenz eines hochaktiven Abbauproduktes des β‐Corticotropins (ACTH) aus Schweinehypophysen. (Vorläufige Mitteilung)
Author(s) -
Kappeler H.,
Schwyzer R.
Publication year - 1961
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.19610440436
Subject(s) - chemistry , trifluoroacetic acid , yield (engineering) , hydrolysate , stereochemistry , peptide , derivative (finance) , amino acid , hydrolysis , organic chemistry , biochemistry , materials science , economics , financial economics , metallurgy
A tetracosapeptide (11) incorporating the amino acid residues 1–24 of β‐corticotropin has been synthesized. This peptide was held responsible for the ACTH‐activity in acid hydrolysates of porcine β‐corticotropin, but was never isolated therefrom. The synthesis was made possible by using N ε ‐ t ‐butoxycarbonyl‐ L ‐lysine and γ‐ t ‐butyl‐ L ‐glutamate as intermediates. A number of other key‐intermediates were prepared as their p ‐phenylazo‐benzyloxy‐carbonyl derivatives, the colour facilitating purification. As in the preparation of an analogous nonadecapeptide, the last condensation involved a crystalline derivative of the decapeptide sequence 1 – 10 . Removal of all protecting groups in the last step ( t ‐butoxy‐carbonyl‐ and t ‐butoxy‐) was effected in quantitative yield by dissolution in trifluoroacetic acid.