Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Patent
1995-03-22
1999-02-23
Tsang, Cecilia J.
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
536112, 514 2, 525 542, C08B 3702
Patent
active
058745696
DESCRIPTION:
BRIEF SUMMARY
The present invention relates to a method of modifying the binding properties of the surface of a solid phase on which nucleophilic groups are present, a method of immobilizing a chemical compound to the surface of a solid phase, and the solid phase modified by the method in the form of an article, and the use thereof in solid phase reactions.
THE TECHNICAL FIELD
Immobilization of various chemical compounds to surfaces of solid phases, such as glass and plastic materials or other solid materials, is used in a variety of chemical and biochemical techniques in which the chemical compound is bound to the surface of the solid phase, in order to be able at this locality to form part of solid phase reactions with other chemical compounds. Such solid phase reactions occur e.g. within chromatography, solid phase assays, including biosensors and solid phase peptide and oligonucleotide synthesis, and they are also used in bioreactors. Further, solid phase reactions occur e.g. in chemical surface treatment of biological surfaces, such as teeth, as a step in glueing items thereon.
Methods of immobilizing chemical compounds to solid phases are multifarious and depend on the object, but within the fields of application mentioned below the present invention constitutes a clear improvement over the existing techniques, since e.g. the durability of immobilized proteins is improved, the functionality is retained, and it is possible to recognize/immobilize peptides.
DESCRIPTION OF THE KNOWN ART
Use of solid phase assay technique, including Enzyme Linked Immunosorbent Assays (ELISA) (Engvall E. and Perlmann P. "Enzyme-linked immunosorbent assay, ELISA. Quantitation of specific antibodies by enzyme-labeled anti-immunoglobulin in antigene-coated tubes", J. Immunol, 109: 129-35, 1972) and solid phase radioimmunoassays (RIA), has during recent years been growing strongly for concentration determination of both antigenes and antibodies. Furthermore solid phase assays and the appertaining radioactive or non-radioactive detection systems are used in gene probe based hybridization assays and in biosensors.
By conventional ELISA or solid phase-RIA-technique antigenes/antibodies are most often immobilized to the solid phase by passive adsorption. Certain proteins, peptides, polysaccharides, haptenes and oligo-/polynucleotides can, however, not be immobilized/detected in this way, and other compounds are denatured and destroyed in the adsorption process (Kurki P. and Virtanen I. "The detection of human antibodies against cytoskeletal components". J. Immunol. Methods, 67: 209-23, 1984).
Further, the orientation of the antigene after immobilization to the solid phase may in certain cases be such that some parts are sterically hindered against interaction with e.g. the antibody. Finally, there may in several cases be a number of serious problems of unspecific (and undesired) binding of the succeeding (maybe enzyme- or isotope-labeled) compounds in the ELISA-or RIA-methods.
Some of the problems can be overcome by methods where the micro-titre-plate is chemically modified with functional groups, whereafter non-adsorbing molecules can be bound covalently by conventional cross-linking technology (cf. e.g. Neurath, A R and Strick, N "Enzyme-linked fluorescence immunoassays using beta-galactosidase and antibodies covalently bound to polystyrene plates. J. Virol. Methods. 3: 155-65, 1981, and e.g. GlueTech Aps "A method for covalent fixation of molecules on a solid phase", WO89/05329).
Often, however, this does not solve the problems of denaturing and consequently deterioration of the quality of the immobilized oligo-/polypeptides or oligo-/polynucleotides, since the hydrophobic solid surface is still present. Furthermore, the technique requires quite some chemical expertise on the part of the performer, since use must be made of biofunctional cross-linking reagents. This is also so if the problem is sought solved by non-adsorbing molecules, such as e.g. peptides, being conjugated to larger proteins before the latter subsequently are adsorb
REFERENCES:
patent: 4959306 (1990-09-01), Kameda et al.
patent: 4975532 (1990-12-01), Rowley et al.
patent: 5030697 (1991-07-01), Hugl
patent: 5116962 (1992-05-01), Stuber et al.
patent: 5198493 (1993-03-01), Holmberg
patent: 5240994 (1993-08-01), Brink
patent: 5516673 (1996-05-01), Margel
Caruthers, Some Modern Methods of Ong Syn pp. 348-350, 1978.
Groman, TIBTECH 5, 220, 1987.
Hermanson, Immobilized Affinity Ligand Techniques 85-88, 144, 145, 214 (1992).
Nilsson (Meth Enzymol 135, 65-78, 1987).
Elsner Henrik
Mouritsen S.o slashed.ren
Lukton David
Mouritsen & Elsner A/S
Tsang Cecilia J.
LandOfFree
Method of preparing tresyl-activated dextran, article having tre does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Method of preparing tresyl-activated dextran, article having tre, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method of preparing tresyl-activated dextran, article having tre will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-308422