Selection of Galectin-Binding Ligands from Synthetic Glycopeptide Libraries

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F23%3A43927819" target="_blank" >RIV/60461373:22330/23:43927819 - isvavai.cz</a>

Výsledek na webu

<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cplu.202300567" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cplu.202300567</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cplu.202300567" target="_blank" >10.1002/cplu.202300567</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Selection of Galectin-Binding Ligands from Synthetic Glycopeptide Libraries

Popis výsledku v původním jazyce

Galectins, a class of carbohydrate-binding proteins, play a crucial role in various physiological and disease processes. Therefore, the identification of ligands that efficiently bind these proteins could potentially lead to the development of new therapeutic compounds. In this study, we present a method that involves screening synthetic click glycopeptide libraries to identify lectin-binding ligands with low micromolar affinity. Our methodology, initially optimized using Concanavalin A, was subsequently applied to identify binders for the therapeutically relevant galectin 1. Binding affinities were assessed using various methods and showed that the selected glycopeptides exhibited enhanced binding potency to the target lectins compared to the starting sugar moieties. This approach offers an alternative means of discovering galectin-binding ligands as well as other carbohydrate-binding proteins, which are considered important therapeutic targets.

Název v anglickém jazyce

Selection of Galectin-Binding Ligands from Synthetic Glycopeptide Libraries

Popis výsledku anglicky

Galectins, a class of carbohydrate-binding proteins, play a crucial role in various physiological and disease processes. Therefore, the identification of ligands that efficiently bind these proteins could potentially lead to the development of new therapeutic compounds. In this study, we present a method that involves screening synthetic click glycopeptide libraries to identify lectin-binding ligands with low micromolar affinity. Our methodology, initially optimized using Concanavalin A, was subsequently applied to identify binders for the therapeutically relevant galectin 1. Binding affinities were assessed using various methods and showed that the selected glycopeptides exhibited enhanced binding potency to the target lectins compared to the starting sugar moieties. This approach offers an alternative means of discovering galectin-binding ligands as well as other carbohydrate-binding proteins, which are considered important therapeutic targets.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10401 - Organic chemistry

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

ChemPlusChem

ISSN

2192-6506

e-ISSN

2192-6506

Svazek periodika

neuveden

Číslo periodika v rámci svazku

2023-12-06

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

001108728200001

EID výsledku v databázi Scopus

2-s2.0-85178277997