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Circular dichroism and conformational analysis of the membrane‐modifying peptide ‐ N ‐ t ‐Boc‐(Aib‐ L ‐Ala) 5 ‐Gly‐Ala‐Aib‐Pro‐Ala‐Aib‐Aib‐Glu‐(OBzl)‐Gln‐OMe with respect to alamethicin
Author(s) -
Oekonomopulos R.,
Jung G.
Publication year - 1980
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1980.360190114
Subject(s) - alamethicin , chemistry , circular dichroism , stereochemistry , peptide , helix (gastropod) , membrane , biochemistry , ecology , lipid bilayer , snail , biology
The conformational analysis of the CD spectrum is reported for the synthetic and membrane‐modifying nonadecapeptide analog of alamethicin N ‐ t ‐Boc‐(Aib‐ L ‐Ala) 5 ‐Gly‐Ala‐Aib‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐ Gln‐OMe. The CD data are evaluated according to three different methods and are discussed with respect to those obtained from natural alamethicin and suitable models such as N ‐ t ‐Boc‐(Aib‐ L ‐Ala) 7 ‐OPOE, fragments of the synthetic nonadecapeptide, and the hexadecapeptide N ‐ t ‐Boc‐(Aib‐ L ‐Ala) 5 ‐Pro‐Ala‐Aib‐Aib‐Glu(OBzl)‐Gln‐OMe. The synthetic nonadecapeptide with the longer helical region exhibits membrane activities comparable to those of alamethicin, whereas the hexadecapeptide with the shorter helix is inactive.