Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1

Ryo Inoue, Kentarou Watanabe, Toyofusa Katou, Yasunori Ikezawa, Keita Hamasaki

Research output: Contribution to journal › Article

7 Citations (Scopus)

Abstract

Nucleobase modified neamines with a lysine as the linker (NbK-neamines) were synthesized and their binding toward hairpin RNAs derived from HIV-1 activator region were studied. NbK-neamines were bind those RNAs with micro molar level of binding affinities and compete with corresponding activator peptide for TAR RNA, but not for RRE RNA. GbK-neamine denotes the highest binding affinity with TAR RNA, three to five times higher than other three NbK-neamines. GbK-neamine could be a candidate of potential inhibitor for TAR-Tat.

Original languageEnglish
Pages (from-to)2139-2147
Number of pages9
JournalBioorganic and Medicinal Chemistry
Volume23
Issue number9
DOIs
Publication statusPublished - 2015 May 1

Fingerprint

Lysine
RNA
neamine
Peptides

Keywords

  • Aminoglycoside
  • Neamine
  • Nucleobase
  • Potential inhibitor
  • RRE RNA
  • TAR RNA

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1. / Inoue, Ryo; Watanabe, Kentarou; Katou, Toyofusa; Ikezawa, Yasunori; Hamasaki, Keita.

In: Bioorganic and Medicinal Chemistry, Vol. 23, No. 9, 01.05.2015, p. 2139-2147.

Research output: Contribution to journal › Article

Inoue, R, Watanabe, K, Katou, T, Ikezawa, Y & Hamasaki, K 2015, 'Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1', Bioorganic and Medicinal Chemistry, vol. 23, no. 9, pp. 2139-2147. https://doi.org/10.1016/j.bmc.2015.03.001
Inoue R, Watanabe K, Katou T, Ikezawa Y, Hamasaki K. Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1. Bioorganic and Medicinal Chemistry. 2015 May 1;23(9):2139-2147. https://doi.org/10.1016/j.bmc.2015.03.001
Inoue, Ryo ; Watanabe, Kentarou ; Katou, Toyofusa ; Ikezawa, Yasunori ; Hamasaki, Keita. / Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1. In: Bioorganic and Medicinal Chemistry. 2015 ; Vol. 23, No. 9. pp. 2139-2147.
@article{19ed9a02e1b2412fa5f3b9332cb15d9a,
title = "Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1",
abstract = "Nucleobase modified neamines with a lysine as the linker (NbK-neamines) were synthesized and their binding toward hairpin RNAs derived from HIV-1 activator region were studied. NbK-neamines were bind those RNAs with micro molar level of binding affinities and compete with corresponding activator peptide for TAR RNA, but not for RRE RNA. GbK-neamine denotes the highest binding affinity with TAR RNA, three to five times higher than other three NbK-neamines. GbK-neamine could be a candidate of potential inhibitor for TAR-Tat.",
keywords = "Aminoglycoside, Neamine, Nucleobase, Potential inhibitor, RRE RNA, TAR RNA",
author = "Ryo Inoue and Kentarou Watanabe and Toyofusa Katou and Yasunori Ikezawa and Keita Hamasaki",
year = "2015",
month = "5",
day = "1",
doi = "10.1016/j.bmc.2015.03.001",
language = "English",
volume = "23",
pages = "2139--2147",
journal = "Bioorganic and Medicinal Chemistry",
issn = "0968-0896",
publisher = "Elsevier Limited",
number = "9",

}

TY - JOUR

T1 - Nucleobase modified neamines with a lysine as a linker, their inhibition specificity for TAR-Tat derived from HIV-1

AU - Inoue, Ryo

AU - Watanabe, Kentarou

AU - Katou, Toyofusa

AU - Ikezawa, Yasunori

AU - Hamasaki, Keita

PY - 2015/5/1

Y1 - 2015/5/1

N2 - Nucleobase modified neamines with a lysine as the linker (NbK-neamines) were synthesized and their binding toward hairpin RNAs derived from HIV-1 activator region were studied. NbK-neamines were bind those RNAs with micro molar level of binding affinities and compete with corresponding activator peptide for TAR RNA, but not for RRE RNA. GbK-neamine denotes the highest binding affinity with TAR RNA, three to five times higher than other three NbK-neamines. GbK-neamine could be a candidate of potential inhibitor for TAR-Tat.

AB - Nucleobase modified neamines with a lysine as the linker (NbK-neamines) were synthesized and their binding toward hairpin RNAs derived from HIV-1 activator region were studied. NbK-neamines were bind those RNAs with micro molar level of binding affinities and compete with corresponding activator peptide for TAR RNA, but not for RRE RNA. GbK-neamine denotes the highest binding affinity with TAR RNA, three to five times higher than other three NbK-neamines. GbK-neamine could be a candidate of potential inhibitor for TAR-Tat.

KW - Aminoglycoside

KW - Neamine

KW - Nucleobase

KW - Potential inhibitor

KW - RRE RNA

KW - TAR RNA

UR - http://www.scopus.com/inward/record.url?scp=84939994352&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84939994352&partnerID=8YFLogxK

U2 - 10.1016/j.bmc.2015.03.001

DO - 10.1016/j.bmc.2015.03.001

M3 - Article

C2 - 25819332

AN - SCOPUS:84939994352

VL - 23

SP - 2139

EP - 2147

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

SN - 0968-0896

IS - 9

ER -

Access to Document