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Sequence dependence of secondary‐structure formation part IV Helix‐forming potential of amphiphilic oligopeptides containing aib residues
Author(s) -
Mutter Manfred,
Altmann KarlHeinz,
Flörsheimer Andreas,
Herbert JüRgen
Publication year - 1986
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.19860690405
Subject(s) - chemistry , oligopeptide , amphiphile , helix (gastropod) , peptide , stereochemistry , circular dichroism , crystallography , organic chemistry , biochemistry , ecology , snail , copolymer , biology , polymer
The conformational properties of Aib‐containing oligopeptides having the propensity to adopt amphiphilic helical conformations were investigated by CD spectroscopy in solution. The peptides CF 3 COOH.H‐Pro‐Glu‐[Ala‐Aib‐Glu‐Aib‐] 4 Gly‐OH ( I ), HCl.H‐Pro‐Ala‐Aib‐[Gul‐Ala‐Ala‐Aib‐] 2 Glu‐Ala‐Aib‐Gly‐PEGM ( II ), and CF 3 COOH.H‐Ala‐Aib‐[Glu‐Glu‐Ala‐Aib‐] 3 PEGM ( III ) were synthesized according to the general principles of the liquid‐phase method for peptide synthesis. Peptides I‐III exhibit helical conformations in CF 3 CH 2 OH, MeOH, and in H 2 O at acidic pH; however, at pH 7, only II forms a stable helix, whereas I and III are predominantly in an unordered conformation. Some general features for the construction of amphiphilic helices are discussed in the light of the experimental data.