Structure-function studies of motilin analogues
作者： Paul Miller , Diane Gagnon , Martin Dickner , Patrice Aubin , Serge St-Pierre
DOI: 10.1016/0196-9781(94)00148-Y
关键词: Receptor 、 Active site 、 Peptide bond 、 Biology 、 Amino acid 、 Motilin 、 Helix 、 Amphiphile 、 Stereochemistry 、 Biochemistry 、 In vitro
摘要: Abstract Over 100 motilin fragments and analogues, including monosubstituted C -terminaldeleted conformationally restricted analogues with peptide bond isoteres (CH 2 -NH), N -terminal adjunct to an amphiphilic helix, were synthesized by solid-phase methodology, purified reverse-phase HPLC, assayed in vitro a muscle strip bioassay (rabbit duodenum) radioligand binding assay on crude membrane extracts from smooth antrum). The data suggest the existence of three distinct regions involved interaction its receptor: region (amino acids 1–7) constitutes minimal basic unit activity; transition acidsa 8–9) links regions; 10–22) forms α-helix that stabilizes residues at active site.
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