Structure and affinity of DNA binding peptides.
Artificial peptides designed to form alpha-helical, beta-turn, antiparallel beta-sheet and beta-hairpin structures which are among the motifs most frequently found in natural DNA/RNA binding proteins were synthesized and their characteristic features were examined in the presence or absence of double or triple stranded DNA by means of UV melting experiments, CD spectra, SPR measurements. It was revealed that amphiphilic character arising from the specific secondary structures and positive charge in the hydrophobic face of peptides played an important role in the interaction with DNA, and that hybrid duplex and triplex were intensively stabilized by the cationic amphiphilic peptides. It was also found that these peptides could protect dsDNA against DNase 1 digestion. These results indicate that structurally designed amphiphilic peptides synthesized in the present study can be powerful tools for antisense and antigene strategies.
Kubo
T
T
Department of Chemistry, Kyushu School of Engineering, Kinki University, 11-6 Kayanomori, Iizuka, Fukuoka 820-8555, Japan.
Yokoyama
K
K
Ueki
R
R
Abe
S
S
Goto
K
K
Niidome
T
T
Aoyagi
H
H
Iwakuma
K
K
Ando
S
S
Ono
S
S
Fujii
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet
D004268:DNA-Binding Proteins; D010455:Peptides; D004247:DNA