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Transfer of peptide hormones from aqueous to membrane phases
Author(s) -
Deber Charles M.,
Behnam Basil A.
Publication year - 1985
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.360240110
Subject(s) - chemistry , phospholipid , membrane , peptide , amphiphile , pentapeptide repeat , enkephalin , biophysics , micelle , nuclear magnetic resonance spectroscopy , biological membrane , aqueous solution , biochemistry , stereochemistry , receptor , organic chemistry , opioid , copolymer , biology , polymer
Peptide hormones and neurotransmitters are functional amphiphilic substances that deploy their chared and nonpolar substituents as required for traversing aqueous phases en rout to their ultimate transfer into the lipid‐rich environment of their membrane‐embedded receptors. As a means of determining the role(s)that cellular membrane lipids may play in mediating these events, we describe an experimental approach, using high‐resolution 1 H‐and 13 C‐nmr spectroscopy, for delineation of the structures of complexes between the (neurotransmitter pentapeptide) enkephalins and micellar and vesicular phospholipid particles. Residue‐specific enkephalin interactions with lipid are identified; affinity constants for the hydrophobic component(s) of peptide/lipid association are calculated for enkephalin and several of its analogs; and comparisons with morphine are presented. Finally, based on molecular details obtained from nmr experiments, a model is proposed for the encoutner of a peptide hormone with a phospholipid membrane surface.