A classification of peptide ligands based on their predicted receptor conformation.
Peptides containing fewer than 50 amino acids show little ordered structure under physiological conditions. In this paper it is shown that in the receptor environment, secondary structure could be induced in small peptides that involves 87% of all the amino acid residues. The statistical methods of Chou and Fasman are used to predict the conformation of 41 peptide hormones or neuromodulators in the proteinaceous environment of the receptor, and four distinct conformational groupings are elucidated. beta-bend, beta-structure and alpha-helical conformation are possible for distinct groups of linear peptides, and disulfide bridge containing peptides show a common beta-bend beta-structure conformation at the receptor. In the predicted receptor conformation, the peptides show hydrophobic and hydrophilic domains that must reflect the distribution of corresponding regions in the ligand-binding site of the receptor. The predicted ligand conformation should allow a more rational approach to interpreting existing structure activity studies and the design of new analogs of pharmacological interest.
D000818:Animals; D004220:Disulfides / Q000032:analysis; D006728:Hormones / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013329:Structure-Activity Relationship
D004220:Disulfides; D006728:Hormones; D008024:Ligands; D010455:Peptides; D011956:Receptors, Cell Surface