Innovative analytical system for screening on lectins.

Lectins are proteins or glycoproteins from plants, animals or microorganisms, which typically bind specifically to sugar residues, e.g., those located in cell walls or membranes. This reaction might change the physiology of the cell wall and influences the metabolism inside the cell. Some lectins of plants stimulate the immune system by unspecific activation of T-cells or influence cell division; others cause agglutination of cells (e.g., erythrocytes) and are therefore from therapeutic interest. In a new approach, biomolecular interaction analysis (BIA) was utilized for a screening program on lectins. The BIA has been done by a new interferometric biosensor based on spectral-phase interference (SPI). The system can be used either for characterisation of lectin binding domains or for a screening on lectins obtained from natural sources. Several lectin binding surfaces on the basis of SPI have been established.

[1]  Laura L Kiessling,et al.  Surface plasmon resonance imaging studies of protein-carbohydrate interactions. , 2003, Journal of the American Chemical Society.

[2]  H. Gabius,et al.  Plant lectins: Occurrence, biochemistry, functions and applications , 2001, Glycoconjugate Journal.

[3]  E. Kabat,et al.  Studies on specificity and binding properties of the blood group A reactive hemagglutinin from Helix pomatia. , 1971, Biochemistry.

[4]  H. Franz,et al.  Isolation and properties of three lectins from mistletoe (Viscum album L.). , 1981, The Biochemical journal.

[5]  P. Edwards,et al.  Determination of association rate constants by an optical biosensor using initial rate analysis. , 1997, Analytical biochemistry.

[6]  I. Goldstein,et al.  PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES. , 1965, Biochemistry.

[7]  N. Sharon,et al.  Lectins as cell recognition molecules. , 1989, Science.

[8]  H. Stauder,et al.  Mistletoe Extracts Standardised in terms of Mistletoe Lectins (ML I) in Oncology: Current State of Clinical Research , 2002, Oncology Research and Treatment.

[9]  M. V. Valeiko,et al.  Multichannel optical biosensors for label-free high-throughput screening , 2002, SPIE Optics East.

[10]  S. Hammarström STRUCTURE, SPECIFICITY, BINDING PROPERTIES, AND SOME BIOLOGICAL ACTIVITIES OF A BLOOD GROUP A‐REACTIVE HEMAGGLUTININ FROM THE SNAIL HELIX POMATIA * , 1974, Annals of the New York Academy of Sciences.

[11]  Tucker,et al.  A Triclinic Crystal Form of the Lectin Concanavalin A , 1996, Journal of structural biology.

[12]  M. Burger,et al.  Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. , 1974, The Journal of biological chemistry.

[13]  B. Chatterjee,et al.  The lectin from Viscum album L.--isolation, characterization, properties and structure. , 1980, The International journal of biochemistry.

[14]  N. Young,et al.  Studies on a phytohemagglutinin from the lentil. II. Multiple forms of Lens culinaris hemagglutinin. , 1971, The Journal of biological chemistry.

[15]  Petr I. Nikitin,et al.  LASER APPLICATIONS AND OTHER TOPICS IN QUANTUM ELECTRONICS: Spectral-phase interference method for detecting biochemical reactions on a surface , 2000 .

[16]  N. Sharon,et al.  Lectin-carbohydrate interactions , 1991 .