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.
Arnusch
Christopher J
CJ
Utrecht Institute for Pharmaceutical Sciences, Department of Medicinal Chemistry, Utrecht University, PO Box 80082, 3508 TB Utrecht, The Netherlands.
André
Sabine
S
Valentini
Paola
P
Lensch
Martin
M
Russwurm
Roland
R
Siebert
Hans-Christian
HC
Fischer
Marcel J E
MJ
Gabius
Hans-Joachim
HJ
Pieters
Roland J
RJ
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