期刊
GLYCOCONJUGATE JOURNAL
卷 19, 期 3, 页码 175-180出版社
KLUWER ACADEMIC PUBL
DOI: 10.1023/A:1024297623445
关键词
binding specificity; dissociation constant; frontal affinity chromatography coupled to electrospray mass spectrometry; lectin; blood group B trisaccharide derivatives; binding surface; carbohydrate-protein recognition
资金
- PHS HHS [29470] Funding Source: Medline
A novel lectin from the mushroom Marasmius oreades (MOA) has been shown to bind to human blood group B oligosaccharides [1]. In the present work we examine the binding of a series of analogues of the blood group B-trisaccharide, alphaGal(1-3)[alphaFuc(1-2)]betaGal-OR (1, R = (CH2)(8)COOMe). MOA was biotinylated and immobilized on a micro column (9.8 muL) for evaluation by Frontal Affinity Chromatography-Mass Spectrometry (FAC-MS) [2]. The trisaccharide 1 was found to be the epitope needed for maximum recognition (K-d = 3.6 muM). A series of synthetic deoxygenated and O-methylated analogues of the B-trisaccharide (R = OMe) were then screened against the lectin, and the key structural elements for binding were determined. OH-4 of the beta-Gal residue and OH-2 of the a-Gal residue were found to be critical for recognition. The FAC-MS technique also proved powerful in evaluating mixtures of compounds. Since the solution NMR structure and crystal structure of the B-trisaccharide are known [3], we propose the specific surface of the trisaccharide that is recognized by the lectin. Published in 2003.
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