[Evaluation of synthetic peptides for the detection of antibodies against human immunodeficiency virus].

Rev Argent Microbiol

Departamento de Química Orgánica, Facultad de Bioquímica y Ciencias Biológicas, UNL, CC 242, 3000 Santa Fe, Argentina.

Published: January 2004

The serologic diagnosis of human immunodeficiency virus (HIV) infection is currently done by detecting the presence of antibodies against the different antigenic viral proteins through immunoassays and later confirmation by Western blot. Several types of antigens can be used in immunoassays, but recombinant proteins and synthetic peptides are the most frequently used. In this paper, peptides mimicking antigenic regions from p24 (region 196-224), gp41 (region 600-614) and gp120 (region 303-338, Loop V3) proteins of HIV-1 have been used as antigens in an enzyme-linked immunosorbent assay and their reactivity was screened against a panel of positive and negative sera. Six antigenic mixtures containing different amounts of each peptide were prepared, and the one consisting of 1 microgram of gp41-15, 0.5 microgram of p24-1 and 0.5 microgram of gp120-1 per well has shown the best performance to differentiate positive and negative serum samples, with sensitivity and specificity values of 99.18% and 100%, respectively. Considering the potential utilization of this system for screening of HIV infection, it would be relevant to evaluate the additional incorporation of sequences derived from Argentine local circulating viral variants to improve the diagnostic sensitivity of the assay, allowing the development of an ELISA based on specific viral sequences.

Download full-text PDF

Source

Publication Analysis

Top Keywords

synthetic peptides
8
human immunodeficiency
8
hiv infection
8
positive negative
8
[evaluation synthetic
4
peptides detection
4
detection antibodies
4
antibodies human
4
immunodeficiency virus]
4
virus] serologic
4

Similar Publications

Chemical and Enzymatic Mechanosynthesis of Organocatalytic Peptide Materials Based on Proline and Phenylalanine.

ChemSusChem

January 2025

Universidad de Antioquia Facultad de Ciencias Exactas y Naturales, Instituto de Química, Calle 70 No 52-21, Medellín, NA, Medellín, COLOMBIA.

In recent years, mechanosynthesis of peptides through either chemical or enzymatic routes has been accomplished. In part, this advancement has been driven due to the organocatalytic properties of peptide-based biomaterials. In this work, we report the merging of chemical and enzymatic protocols under mechanochemical conditions to synthesize peptide materials based on L-proline and L-phenylalanine.

View Article and Find Full Text PDF

Bioactive Sulfonamides Derived from Amino Acids: Their Synthesis and Pharmacological Activities.

Mini Rev Med Chem

January 2025

Department of Physiology and Pharmacology Vittorio Erspamer, Sapienza University of Rome, 00161, Rome, Italy.

Currently, the synthesis of bioactive sulfonamides using amino acid as a starting reagent has become an area of research interest in organic chemistry. Over the years, an amine-sulfonyl chloride reaction has been adopted as a common step in traditional sulfonamide synthetic methods. However, recent developments have shown amino acids to be better precursors than amines in the synthesis of sulfonamides.

View Article and Find Full Text PDF

Chemistries on the inner leaflet of the cell membrane.

Chem Commun (Camb)

January 2025

Institute of Chemical Biology and Nanomedicine, State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan Provincial Key Laboratory of Biomacromolecular Chemical Biology, College of Chemistry and Chemical Engineering, Hunan University, Changsha, 410082, China.

The cell membrane, characterized by its inherent asymmetry, functions as a dynamic barrier that regulates numerous cellular activities. This Highlight aims to provide the chemistry community with a comprehensive overview of the intriguing and underexplored inner leaflet, encompassing both fundamental biology and emerging synthetic modification strategies. We begin by describing the asymmetric nature of the plasma membrane, with a focus on the distinct roles of lipids, proteins, and glycan chains, highlighting the composition and biofunctions of the inner leaflet and the biological mechanisms that sustain membrane asymmetry.

View Article and Find Full Text PDF

Cyclic peptides are often used as scaffolds for the multivalent presentation of drug molecules due to their structural stability and constrained conformation. We identified a cyclic deca-peptide incorporating lipoamino acids for delivering T helper and B cell epitopes against group A Streptococcus (GAS), eliciting robust humoral immune responses. In this study, we assessed the function-immunogenicity relationship of the multi-component vaccine candidate (referred to as VC-13) to elucidate a mechanism of action.

View Article and Find Full Text PDF

The small GTPase MRAS is a broken switch.

Nat Commun

January 2025

Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, QC, H3T 1J4, Canada.

Intense research on founding members of the RAS superfamily has defined our understanding of these critical signalling proteins, leading to the premise that small GTPases function as molecular switches dependent on differential nucleotide loading. The closest homologs of H/K/NRAS are the three-member RRAS family, and interest in the MRAS GTPase as a regulator of MAPK activity has recently intensified. We show here that MRAS does not function as a classical switch and is unable to exchange GDP-to-GTP in solution or when tethered to a lipid bilayer.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!