Solution structural investigation and conformation-activity relationship of BAM8-22 by NMR and molecular dynamics simulations.
NMR spectroscopy and molecular dynamics simulations show that BAM8-22 (Val(8)-Gly(9)-Arg(10)-Pro(11)-Glu(12)-Trp(13)-Trp(14)-Met(15)-Asp(16)-Tyr(17)-Gln(18)-Lys(19)-Arg(20)-Tyr(21)-Gly(22)) possesses a relatively well-defined alpha-helix extending from Glu(12) to Arg(20), whereas both termini remain highly flexible in aqueous solution. The conformation-activity relationship of BAM8-22 indicates that the integrity of the well-defined alpha-helical structure is essential but not the sole determining factor for its bioactivity.
Lv
Guohua
G
Institute of Biochemistry and Molecular Biology, School of Life Sciences, Lanzhou University, 222 Tianshui South Road, Lanzhou 730000, China.
Dong
Shouliang
S
D000595:Amino Acid Sequence; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D019999:Pharmaceutical Solutions / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D019999:Pharmaceutical Solutions; D011498:Protein Precursors; D004744:Enkephalin, Methionine; C028837:BAM 22P