Abstract
Binding behavior of alanine-based oligopeptides containing four or six cationic lysine residues (K4 and K6) to a dA30-dT30 or dG30-dC30 duplex-immobilized on a 27 MHz quartz-crystal microbalance (QCM) were studied in an aqueous buffer solution. Eight kinds of alanine-based oligopeptides were prepared systematically, in which positions of K residues were changed in the helical structure according to common features in DNA recognition helices of the DNA binding protein. The binding amount (Δm) on a nanogram scale and binding constant (Ka) could be obtained from frequency decreases (mass increases) of the DNA-immobilized QCM. Cationic oligopeptides were confirmed, from circular dichroism (CD) spectra, to form α-helical conformations as a result of the binding to DNA strands with random conformations. Δm and Ka values were greatly affected by ionic strength and the position of cationic K residues of peptides. At the low ionic strength, all peptides can bind with the almost same affinity to DNA strands by electrostatic interactions. At the high ionic strength of 40mM NaCl, oligopeptides with cationic K groups at the one side of the α helix showed larger Δmmax (35 ± 5 ngcm-2) and Ka values (104M-1) than those of oligopeptides having K groups in random positions (Δm = 10 ± 5 ng cm-2 and Ka = 103M-1).
| Original language | English |
|---|---|
| Pages (from-to) | 1609-1616 |
| Number of pages | 8 |
| Journal | Chemistry - A European Journal |
| Volume | 5 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - Jan 1 1999 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
Cite this
Binding behavior of lysine-containing helical peptides to DNA duplexes immobilized on a 27 MHz quartz-crystal microbalance. / Niikura, Kenichi; Matsuno, Hisao; Okahata, Yoshio.
In: Chemistry - A European Journal, Vol. 5, No. 5, 01.01.1999, p. 1609-1616.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding behavior of lysine-containing helical peptides to DNA duplexes immobilized on a 27 MHz quartz-crystal microbalance
AU - Niikura, Kenichi
AU - Matsuno, Hisao
AU - Okahata, Yoshio
PY - 1999/1/1
Y1 - 1999/1/1
N2 - Binding behavior of alanine-based oligopeptides containing four or six cationic lysine residues (K4 and K6) to a dA30-dT30 or dG30-dC30 duplex-immobilized on a 27 MHz quartz-crystal microbalance (QCM) were studied in an aqueous buffer solution. Eight kinds of alanine-based oligopeptides were prepared systematically, in which positions of K residues were changed in the helical structure according to common features in DNA recognition helices of the DNA binding protein. The binding amount (Δm) on a nanogram scale and binding constant (Ka) could be obtained from frequency decreases (mass increases) of the DNA-immobilized QCM. Cationic oligopeptides were confirmed, from circular dichroism (CD) spectra, to form α-helical conformations as a result of the binding to DNA strands with random conformations. Δm and Ka values were greatly affected by ionic strength and the position of cationic K residues of peptides. At the low ionic strength, all peptides can bind with the almost same affinity to DNA strands by electrostatic interactions. At the high ionic strength of 40mM NaCl, oligopeptides with cationic K groups at the one side of the α helix showed larger Δmmax (35 ± 5 ngcm-2) and Ka values (104M-1) than those of oligopeptides having K groups in random positions (Δm = 10 ± 5 ng cm-2 and Ka = 103M-1).
AB - Binding behavior of alanine-based oligopeptides containing four or six cationic lysine residues (K4 and K6) to a dA30-dT30 or dG30-dC30 duplex-immobilized on a 27 MHz quartz-crystal microbalance (QCM) were studied in an aqueous buffer solution. Eight kinds of alanine-based oligopeptides were prepared systematically, in which positions of K residues were changed in the helical structure according to common features in DNA recognition helices of the DNA binding protein. The binding amount (Δm) on a nanogram scale and binding constant (Ka) could be obtained from frequency decreases (mass increases) of the DNA-immobilized QCM. Cationic oligopeptides were confirmed, from circular dichroism (CD) spectra, to form α-helical conformations as a result of the binding to DNA strands with random conformations. Δm and Ka values were greatly affected by ionic strength and the position of cationic K residues of peptides. At the low ionic strength, all peptides can bind with the almost same affinity to DNA strands by electrostatic interactions. At the high ionic strength of 40mM NaCl, oligopeptides with cationic K groups at the one side of the α helix showed larger Δmmax (35 ± 5 ngcm-2) and Ka values (104M-1) than those of oligopeptides having K groups in random positions (Δm = 10 ± 5 ng cm-2 and Ka = 103M-1).
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U2 - 10.1002/(SICI)1521-3765(19990503)5:5<1609::AID-CHEM1609>3.0.CO;2-1
DO - 10.1002/(SICI)1521-3765(19990503)5:5<1609::AID-CHEM1609>3.0.CO;2-1
M3 - Article
AN - SCOPUS:0032914565
VL - 5
SP - 1609
EP - 1616
JO - Chemistry - A European Journal
JF - Chemistry - A European Journal
SN - 0947-6539
IS - 5
ER -