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Synthetische Analoge des Hypertensins. IV. Synthese der kettenhomologen Peptide ( des ‐Asp 1 )‐Val 5 ‐Hypertensin II, ( des ‐Phe 8 )‐Val 5 ‐Hypertensin II‐Asp 1 ‐β‐amid, ( homo ‐Tyr 4 ′)‐Val 5 ‐Hypertensin II und ( homo ‐Tyr 4 ′)‐Val 5 ‐Hypertensin II‐Asp 1 ‐β‐amid
Author(s) -
Riniker B.,
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.19610440311
Subject(s) - chemistry , stereochemistry , peptide , biochemistry
The syntheses of the chain‐homologues of hypertensin, H · Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH, H · Asp(NH 2 )‐Arg‐Val‐Tyr‐Val‐His‐Pro · OH, and H · Asp(R)‐Arg‐Val‐Tyr‐Tyr‐Val‐His‐Pro‐Phe · OH (R −OH and −NH 2 ), are described in detail. A system for the nomenclature of such analogues is proposed. The relative stability of H · Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH, H · Gly‐Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH 2 and H · Asp(R)‐Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH in aqueous solution at 50° over a period of 6 months is discussed: the heptapeptide and Val 5 ‐hypertensin II are very stable under these conditions, but the asparaginyl 1 ‐ and glycyl 1 ‐ compounds lose these residues to an extent of about 10%. A possible mechanism explaining the difference in the behaviour of the aspartyl and the asparaginyl residues is suggested.