Interaction of calmodulin with synthetic deletion peptides of melittin.
The 26-residue peptide melittin present in bee venom has been shown to bind calmodulin tightly. In this study we synthesized the following series of deletion peptides of melittin by the solid-phase method: Mel12, Mel13, Mel14, Mel15, Mel15F. The results of this study show that the deletion peptides Mel14 and Mel15 have almost the same binding activity as the intact native peptide. Each deletion peptide forms a 1:1 complex with calmodulin according to electrophoresis analysis. When the tryptophanyl residue of Mel15 was replaced by the phenylalaninyl residue, the dissociation constant of the peptide-calmodulin complex increased. This shows the importance of the tryptophanyl residue for binding to calmodulin.
Liu
L
L
Institute of Polymer Chemistry, Nankai University, Tianjin, China.
Yan
H
H
Ni
A
A
Cheng
X
X
He
B
B
D000595:Amino Acid Sequence; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D003432:Cross-Linking Reagents; D008555:Melitten / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D010649:Phenylalanine / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014364:Tryptophan / Q000737:chemistry
D002147:Calmodulin; D003432:Cross-Linking Reagents; D010455:Peptides; D008555:Melitten; D010649:Phenylalanine; D014364:Tryptophan