Interference of the galactose-dependent binding of lectins by novel pentapeptide ligands.
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.
Utrecht Institute for Pharmaceutical Sciences, Department of Medicinal Chemistry, Utrecht University, PO Box 80082, 3508 TB Utrecht, The Netherlands.
Christopher J
CJ
Arnusch
Sabine
S
André
Paola
P
Valentini
Martin
M
Lensch
Roland
R
Russwurm
Hans-Christian
HC
Siebert
Marcel J E
MJ
Fischer
Hans-Joachim
HJ
Gabius
Roland J
RJ
Pieters
D000595:Amino Acid Sequence; D004305:Dose-Response Relationship, Drug; D005690:Galactose / Q000737:chemistry / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology
D037102:Lectins; D008024:Ligands; D009842:Oligopeptides; D005690:Galactose