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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F14%3A00228393" target="_blank" >RIV/62156489:43210/14:00228393 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216305:26620/14:PU110418

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 beone 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 microg.mL-1 and limit of quantification of 0.1 microg.mL-1 were estimated.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 beone 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 microg.mL-1 and limit of quantification of 0.1 microg.mL-1 were estimated.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CG - Elektrochemie

OECD FORD obor

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Projekt

<a href="/cs/project/EE2.4.31.0023" target="_blank" >EE2.4.31.0023: Partnerská síť centra excelentního bionanotechnologického výzkumu</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

International Journal of Electrochemical Science

ISSN

1452-3981

e-ISSN

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Svazek periodika

9

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

RS - Srbská republika

Počet stran výsledku

12

Strana od-do

3386-3397

Kód UT WoS článku

336899000004

EID výsledku v databázi Scopus

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