Construction of two-stranded alpha-helix peptides based on influenza virus M1 protein selectively bound to RNA.
Various 2alpha-helix peptides were designed and synthesized based on the RNA-binding region of matrix protein M1 in influenza virus. The binding properties of the peptides to model ssRNA, ssDNA, dsDNA, and virus RNA were examined by the fluorescence studies of a dansyl group incorporated into the peptides. The peptide containing the hydrophilic residues of M1 RNA-binding region bound RNAs selectively.
Kuribayashi
H
H
Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Takahashi
T
T
Nagata
K
K
Ueno
A
A
Mihara
H
H
D000595:Amino Acid Sequence; D008954:Models, Biological; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000378:metabolism
C031540:M-protein, influenza virus; C488936:M1 protein, Influenza A virus; D010455:Peptides; D014763:Viral Matrix Proteins; D012313:RNA