title: A computergraphic determination of the chemotactic peptide preferred conformation.
abstract: Replacement of leucine in the chemotactic peptide For-Met-Leu-Phe by the sterically constrained amino acids alpha-aminoisobutyric acid and aminocyclohexanecarboxylic acid affords compounds of equal or greater activity than the parent. NMR studies indicate that the parent compound is present as a beta-sheet in solution, whereas the analogues prefer a beta-turn. Application of molecular modelling would indicate that the beta-turn conformer is energetically preferable and thus suggests that it is the orientation adopted by the peptides.
authors.affiliation: Department of Pharmacology, Medical College of Virginia, Richmond 23298.
authors.forename: S F
authors.initials: SF
authors.lastname: Semus
authors.forename: E L
authors.initials: EL
authors.lastname: Becker
authors.forename: C
authors.initials: C
authors.lastname: Toniolo
authors.forename: R J
authors.initials: RJ
authors.lastname: Freer
mesh_terms: D003196:Computer Graphics; D003198:Computer Simulation; D006860:Hydrogen Bonding; D009240:N-Formylmethionine Leucyl-Phenylalanine; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D009240:N-Formylmethionine Leucyl-Phenylalanine