A computergraphic determination of the chemotactic peptide preferred conformation.
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.
Semus
S F
SF
Department of Pharmacology, Medical College of Virginia, Richmond 23298.
Becker
E L
EL
Toniolo
C
C
Freer
R J
RJ
D003196:Computer Graphics; D003198:Computer Simulation; D006860:Hydrogen Bonding; D009240:N-Formylmethionine Leucyl-Phenylalanine; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D009240:N-Formylmethionine Leucyl-Phenylalanine