Publication result detail

Spectroscopic and Electrochemical Characterization of CD4 Binding Site of HIV-1 Exterior Envelope gp120

CERNEI, N.; HEGER, Z.; KOPEL, P.; MILOSAVLJEVIĆ, V.; KOMÍNKOVÁ, M.; MOULICK, A.; ZÍTKA, O.; TRNKOVÁ, L.; ADAM, V.; KIZEK, R.

Original Title

Spectroscopic and Electrochemical Characterization of CD4 Binding Site of HIV-1 Exterior Envelope gp120

English Title

Spectroscopic and Electrochemical Characterization of CD4 Binding Site of HIV-1 Exterior Envelope gp120

Type

WoS Article

Original Abstract

Glycoprotein 120 (gp120) is essential biomolecule for HIV-1 entry into cells as it plays a vital role in attachment to specific cell surface receptors. Exterior envelope glycoprotein 120 contains conservative CD4 binding site in its structure that may be one of target molecules for development of HIV therapeutic agents, able to inhibit the viral entry steps into the host cells. The present study describes the solid-phase, Fmoc-based synthesis of CD4 binding site (SSGGD PEIVMH), and its subsequent spectroscopic characterization, with determined purity over 90 %. Moreover; electrochemical analyses were carried out to optimize the conditions for peptide determination. Using the optimized conditions as Britton-Robinson buffer with pH 8 and 3% addition of acetonitrile (v/v) as a mobile phase, potential 1100 mV, limit of detection of 0.04 ug.mL-1 and limit of quantification of 0.1 ug.mL-1 were estimated

English abstract

Glycoprotein 120 (gp120) is essential biomolecule for HIV-1 entry into cells as it plays a vital role in attachment to specific cell surface receptors. Exterior envelope glycoprotein 120 contains conservative CD4 binding site in its structure that may be one of target molecules for development of HIV therapeutic agents, able to inhibit the viral entry steps into the host cells. The present study describes the solid-phase, Fmoc-based synthesis of CD4 binding site (SSGGD PEIVMH), and its subsequent spectroscopic characterization, with determined purity over 90 %. Moreover; electrochemical analyses were carried out to optimize the conditions for peptide determination. Using the optimized conditions as Britton-Robinson buffer with pH 8 and 3% addition of acetonitrile (v/v) as a mobile phase, potential 1100 mV, limit of detection of 0.04 ug.mL-1 and limit of quantification of 0.1 ug.mL-1 were estimated

Keywords

CD4 binding loop; gp120; Human immunodeficiency virus-1; Peptide synthesis

Key words in English

CD4 binding loop; gp120; Human immunodeficiency virus-1; Peptide synthesis

Authors

CERNEI, N.; HEGER, Z.; KOPEL, P.; MILOSAVLJEVIĆ, V.; KOMÍNKOVÁ, M.; MOULICK, A.; ZÍTKA, O.; TRNKOVÁ, L.; ADAM, V.; KIZEK, R.

RIV year

2015

Released

01.07.2014

ISBN

1452-3981

Periodical

International Journal of Electrochemical Science

Volume

9

Number

7

State

Republic of Serbia

Pages from

3386

Pages to

3397

Pages count

12

BibTex

@article{BUT109373,
  author="Natalia Vladimirovna {Cernei} and Zbyněk {Heger} and Pavel {Kopel} and Vedran {Milosavljević} and Markéta {Komínková} and Amitava {Moulick} and Ondřej {Zítka} and Libuše {Trnková} and Vojtěch {Adam} and René {Kizek}",
  title="Spectroscopic and Electrochemical Characterization of CD4 Binding Site of HIV-1 Exterior Envelope gp120",
  journal="International Journal of Electrochemical Science",
  year="2014",
  volume="9",
  number="7",
  pages="3386--3397",
  issn="1452-3981"
}