Search for Peptides Specifically Binding with the B7-2 Costimulatory Molecule

Abstract— The interaction of B7-1/B7-2 ligands with CD28/CTLA-4 receptors plays a key role in the regulation of the immune response. The aim of this study was to find and study peptides that interact with the human B7-2 molecule. In the course of the work, three rounds of affinity selection were carried out and individual phage clones were selected, which include peptides with varying degrees of interaction with the coregulatory target B7-2. As a result of DNA sequencing of selected phages, nucleotide sequences encoding peptides that specifically bind to B7-2 were obtained. The identified peptides can be used as a basis for the development of immunotherapeutic drugs for regulating the immune response in the treatment of oncological diseases.

Lexical Solidarities

In the present study Eugeniu Coşeriu talks about the lexical structures that can be identified in the vocabulary of a language. As the author shows, they can be either paradigmatic or syntagmatic. Paradigmatic structures, in turn, can be primary (lexical fields and lexical classes) or secondary (structures of modification, development, composition), and syntagmatic structures or solidarity can be of three types, conventionally called: affinity, selection and implication.

High-Throughput Affinity Selection Mass Spectrometry Using SAMDI-MS to Identify Small-Molecule Binders of the Human Rhinovirus 3C Protease

Affinity selection mass spectrometry (ASMS) has emerged as a powerful high-throughput screening tool used in drug discovery to identify novel ligands against therapeutic targets. This report describes the first high-throughput screen using a novel self-assembled monolayer desorption ionization (SAMDI)–ASMS methodology to reveal ligands for the human rhinovirus 3C (HRV3C) protease. The approach combines self-assembled monolayers of alkanethiolates on gold with matrix-assisted laser desorption ionization time-of-flight (MALDI TOF) mass spectrometry (MS), a technique termed SAMDI-ASMS. The primary screen of more than 100,000 compounds in pools of 8 compounds per well was completed in less than 8 h, and informs on the binding potential and selectivity of each compound. Initial hits were confirmed in follow-up SAMDI-ASMS experiments in single-concentration and dose–response curves. The ligands identified by SAMDI-ASMS were further validated using differential scanning fluorimetry (DSF) and in functional protease assays against HRV3C and the related SARS-CoV-2 3CLpro enzyme. SAMDI-ASMS offers key benefits for drug discovery over traditional ASMS approaches, including the high-throughput workflow and readout, minimizing compound misbehavior by using smaller compound pools, and up to a 50-fold reduction in reagent consumption. The flexibility of this novel technology opens avenues for high-throughput ASMS assays of any target, thereby accelerating drug discovery for diverse diseases.