Binding behavior of lysine-containing helical peptides to DNA duplexes immobilized on a 27 MHz quartz-crystal microbalance

Kenichi Niikura, Hisao Matsuno, Yoshio Okahata

Research output: Contribution to journalArticle

27 Citations (Scopus)

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 languageEnglish
Pages (from-to)1609-1616
Number of pages8
JournalChemistry - A European Journal
Volume5
Issue number5
DOIs
Publication statusPublished - Jan 1 1999
Externally publishedYes

Fingerprint

Oligopeptides
Quartz crystal microbalances
Peptides
Lysine
DNA
Ionic strength
Alanine
Conformations
Immobilized Nucleic Acids
DNA-Binding Proteins
Dichroism
Coulomb interactions
Buffers

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 journalArticle

@article{60a061ec7d294130a2f0d3eed8783c13,
title = "Binding behavior of lysine-containing helical peptides to DNA duplexes immobilized on a 27 MHz quartz-crystal microbalance",
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).",
author = "Kenichi Niikura and Hisao Matsuno and Yoshio Okahata",
year = "1999",
month = "1",
day = "1",
doi = "10.1002/(SICI)1521-3765(19990503)5:5<1609::AID-CHEM1609>3.0.CO;2-1",
language = "English",
volume = "5",
pages = "1609--1616",
journal = "Chemistry - A European Journal",
issn = "0947-6539",
publisher = "Wiley-VCH Verlag",
number = "5",

}

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).

UR - http://www.scopus.com/inward/record.url?scp=0032914565&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032914565&partnerID=8YFLogxK

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 -