Abstract
This paper describes the single channel properties of a series of synthetic analogues of gramicidin A, where all four tryptophans are replaced either by tyrosine or by several O-protected (benzyl, methyl, ethyl or t-butyl) derivatives. It is shown that, although all analogues bear similar dipole moment on their side-chains, the conductance depends on the hydrophobicity of these protecting groups. An analysis of the conductance data suggests that the conductance is governed by the binding process and a possible explanation, based on conformational considerations, is proposed.
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Abbreviations
- GA:
-
X=tryptophane
- GM:
-
X=phenylalanine
- GN:
-
X=naphthylalanine
- GQ8:
-
X=8-quinolylalanine
- GQ4:
-
X=4-quinolylalanine
- GT:
-
X=tyrosine
- GTBzl:
-
X=O-benzyltyrosine
- GTMe:
-
X=O-methyltyrosine
- GTEt:
-
X=O-ethyltyrosine
- GTBu:
-
X=O-t-butyltyrosine
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Benamar, D., Daumas, P., Trudelle, Y. et al. Influence of the nature of the aromatic side-chain on the conductance of the channel of linear gramicidin: study of a series of 9,11,13,15-Tyr(O-protected) derivatives. Eur Biophys J 22, 145–150 (1993). https://doi.org/10.1007/BF00196918
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DOI: https://doi.org/10.1007/BF00196918