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Structural investigation of poly‐ L , D ‐proline, a synthetic ion channel across bilayer membranes: Crystal structure and molecular conformation of two tetra‐ D , L ‐proline derivatives
Author(s) -
Colapietro M.,
De Santis P.,
Palleschi A.,
Spagna R.
Publication year - 1986
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.360251202
Subject(s) - chemistry , bilayer , proline , tetra , membrane , peptide , stereochemistry , crystal structure , crystallography , lipid bilayer , ion , residue (chemistry) , ion channel , amino acid , organic chemistry , biochemistry , receptor , medicinal chemistry
The crystal structures and molecular conformations of two tetraproline derivatives with alternating configurations Boc( D ‐Pro, L ‐Pro) 2 OH and Boc( D ‐Pro, L ‐Pro) 2 OCH 3 are investigated in connection with the ability of the homologous polymer to selectively increase (as an ion channel) the ion permeability across bilayer membranes. Both tetramers are characterized by the cis ‐ trans alternating conformation of the peptide bonds, which formally transforms in a turn of the poly‐ D , L ‐proline channel after a cis ‐ trans change of the central peptide residue.