Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Christopher J. Arnusch; Sabine André; Paola Valentini; Martin Lensch; Roland Russwurm; Hans-Christian Siebert; Marcel J. E. Fischer; Hans-Joachim Gabius; Roland J. Pieters

doi:10.1016/j.bmcl.2004.01.029

Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Christopher J. Arnusch, Sabine André, Paola Valentini, Martin Lensch, Roland Russwurm, Hans-Christian Siebert, Marcel J. E. Fischer, Hans-Joachim Gabius, Roland J. Pieters

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3 times stronger than galactose and NMR studies suggested real carbohydrate mimicry. © 2004 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	1437-1440
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	14
Issue number	6
DOIs	https://doi.org/10.1016/j.bmcl.2004.01.029
Publication status	Published - 22 Mar 2004

Keywords

carbohydrate
galactose
galectin
lectin
ligand
pentapeptide
amino acid sequence
article
library
nuclear magnetic resonance
protein analysis
protein binding
protein modification

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10.1016/j.bmcl.2004.01.029

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title = "Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands",

abstract = "A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3 times stronger than galactose and NMR studies suggested real carbohydrate mimicry. {\textcopyright} 2004 Elsevier Ltd. All rights reserved.",

keywords = "carbohydrate, galactose, galectin, lectin, ligand, pentapeptide, amino acid sequence, article, library, nuclear magnetic resonance, protein analysis, protein binding, protein modification",

author = "Arnusch, {Christopher J.} and Sabine Andr{\'e} and Paola Valentini and Martin Lensch and Roland Russwurm and Hans-Christian Siebert and Fischer, {Marcel J. E.} and Hans-Joachim Gabius and Pieters, {Roland J.}",

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T1 - Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

AU - Arnusch, Christopher J.

AU - André, Sabine

AU - Valentini, Paola

AU - Lensch, Martin

AU - Russwurm, Roland

AU - Siebert, Hans-Christian

AU - Fischer, Marcel J. E.

AU - Gabius, Hans-Joachim

AU - Pieters, Roland J.

PY - 2004/3/22

Y1 - 2004/3/22

N2 - A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3 times stronger than galactose and NMR studies suggested real carbohydrate mimicry. © 2004 Elsevier Ltd. All rights reserved.

AB - A library of pentapeptides containing the sequence -Y-X-Y- based on rational design was screened with six different lectins. Sequences were identified that modulate galectin binding to its natural carbohydrate ligand. SPR showed inhibition values 2-3 times stronger than galactose and NMR studies suggested real carbohydrate mimicry. © 2004 Elsevier Ltd. All rights reserved.

KW - carbohydrate

KW - galactose

KW - galectin

KW - lectin

KW - ligand

KW - pentapeptide

KW - amino acid sequence

KW - article

KW - library

KW - nuclear magnetic resonance

KW - protein analysis

KW - protein binding

KW - protein modification

U2 - 10.1016/j.bmcl.2004.01.029

DO - 10.1016/j.bmcl.2004.01.029

M3 - Article

SN - 0960-894X

VL - 14

SP - 1437

EP - 1440

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 6

ER -

Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands

Abstract

Keywords

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