Publication details
Spectroscopic and electrochemical characterization of CD4 binding site of HIV-1 exterior envelope gp120
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Article in Periodical |
| Magazine / Source | International journal of electrochemical science |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.electrochemsci.org/papers/vol9/90703386.pdf |
| Field | Physical chemistry and theoretical chemistry |
| Keywords | CD4 binding loop; gp120; Human immunodeficiency virus-1; peptide synthesis |
| Description | 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 mu g.mL(-1) and limit of quantification of 0.1 mu g.mL(-1) were estimated. |