title: Cyclopeptides of Linum usitatissimum.
abstract: Cyclolinopeptide A (CLA), a cyclic nonapeptide from linseed, possesses strong immunosuppressive and antimalarial activity along with the ability to inhibit cholate uptake into hepatocytes. The structure of the peptide was studied extensively in solution as well as in the solid state. It is postulated that both the Pro-Pro cis-amide bond and an 'edge-to-face' interaction between the aromatic rings of two adjacent Phe residues are important for biological activity. Structure-activity relationship studies of many linear and cyclic analogues of CLA suggest that the Pro-Xxx-Phe sequence and the flexibility of the peptide are important for the immunosuppressive activity.
authors.affiliation: Faculty of Chemistry, University of Wroclaw, 14 F. Joliot-Curie, 50-383 Wroclaw, Poland.
authors.forename: Bolesław
authors.initials: B
authors.lastname: Picur
authors.forename: Marek
authors.initials: M
authors.lastname: Cebrat
authors.forename: Janusz
authors.initials: J
authors.lastname: Zabrocki
authors.forename: Ignacy Z
authors.initials: IZ
authors.lastname: Siemion
mesh_terms: D000595:Amino Acid Sequence; D019597:Flax / Q000737:chemistry*; D007166:Immunosuppressive Agents / Q000737:chemistry*; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D011392:Proline / Q000737:chemistry; D012639:Seeds / Q000737:chemistry; D013329:Structure-Activity Relationship
chemical_list: D007166:Immunosuppressive Agents; D010456:Peptides, Cyclic; C055018:cyclolinopeptide A; D010649:Phenylalanine; D011392:Proline