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MXPA96006584A - Sensitive biosensors to ma - Google Patents

Sensitive biosensors to ma

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Publication number
MXPA96006584A
MXPA96006584AMXPA/A/1996/006584AMX9606584AMXPA96006584AMX PA96006584 AMXPA96006584 AMX PA96006584AMX 9606584 AMX9606584 AMX 9606584AMX PA96006584 AMXPA96006584 AMX PA96006584A
Authority
MX
Mexico
Prior art keywords
solid phase
sensor
participant
process according
coated
Prior art date
Application number
MXPA/A/1996/006584A
Other languages
Spanish (es)
Other versions
MX9606584A (en
Inventor
Meller Paul
Wiegand Andreas
Madry Norbert
Schelp Carsten
Mohlen Michael
Original Assignee
Dade Behring Marburg Gmbh
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Priority claimed from DE19548376Aexternal-prioritypatent/DE19548376A1/en
Application filed by Dade Behring Marburg GmbhfiledCriticalDade Behring Marburg Gmbh
Publication of MXPA96006584ApublicationCriticalpatent/MXPA96006584A/en
Publication of MX9606584ApublicationCriticalpatent/MX9606584A/en

Links

Abstract

The present invention relates to a piezoelectric sensor for use in diagnostic and analysis procedures, especially for the immunochemical testing of specific binders relevant for diagnosis.

Description

SENSITIVE BLOCKS TO MASSES.
The present invention relates to a p-sensor, zoelectric for use in diagnostic / analytical procedures, especially for the immunochemical identification of specific binding partners, of relevance in diagnosis. Piezoelectric sensors as such are known, for example, from Dickert et al. (Che ie in unserer Zeit 28 (3), pages 147-152 (1994)). Such biosensors are also disclosed, for example, in U.S. Pat. 4,236,893 and 4,735,906. Such biosensors, which can be used for the identification of molecules of relevance in diagnosis (analysts), are usually composed of a transducer with a surface coated with a specific binding partner for the molecule to be identified, thereby it is able to selectively bind these molecules. Most often quartz piezoelectric crystals are used as a transducer. If the quartz crystal is mounted on a suitable electronic switching circuit, then it vibrates at a certain resonance frequency. If then the molecules to be identified accumulate, then the resonance frequency shifts. Such electronic switching circuits are known to the person skilled in the art, for example from DE-A 39 20 052. Even though these known biosensors already partially satisfy the functions assigned to them, it is nevertheless demonstrated that, in the methods employed in which they are attached to the quartz surface, for example, anti-bodies through silane derivatives, on the one hand that the procedure for the binding of the antibodies to the quartz surface is very complex and difficult to repress. on the other hand, that the procedure of the surface of the sensor by treatment with a reactive agent that must break the union between the antigen to be identified and the antibodies and separate the bound antigen is, on the other hand, hardly reproducible and leads to an uncontrolled degradation of the antibodies on the surface of the sensor. In a DAVI publication? et al. (Anal. Che. (1989), 61 (11), pages 1227-1230 it is described that the transducer can be coated with gold and bound to this protein A layer. Protein A, on the other hand, can reversibly bind antibodies for identification of molecules of relevance in diagnosis As the authors themselves conclude, by means of the coating with protein A the signal is strongly displaced and the measurement is made difficult, therefore, the present invention has as its mission to propose a biosensor for use in analytical procedures or diagnostic, which can be simply coated with a specific binding partner at the same time, must be regenerated in a simple and safe manner after the specific reaction has elapsed.This problem is solved according to the present invention by covering the sensor with a noble metal, preferably gold and being able to bind to this coating a participant in the specific union. This way the participant in the specific union can be separated, for example by the reagents known from DE 44 36 910. It is not essential for the present invention in which form of execution the transducer is or in what form and manner the change caused by the accumulation of analytes it becomes a measurement signal. The present invention can be used both in manual procedures in which, for example, the sensor is immersed in the r-ertri, as well as in automatic analysis devices. Basically, the procedure according to 1? The invention can be carried out in the following manner: a commercially available gold-coated pi-ezoelectric crystal -which is integrated in an integrated electronic switching circuit- (for example from the company Sepsotec), is coated with a participant in the specific binding for the analyte to be determined. A participant in the specific union of this type can be, for example, an antibody or monoclonal or polyclonal antibody fragment, a lectin or an antigen. The coating duration can range between 5 min and several hours, preferably between 10 and 120 min. After the coating the sensor surface is rinsed with washing buffer. The washing buffer preferably has a detergent. Optionally, after the specific coating, an inespecific coating can also be carried out, for example with inactivated BSA or POD, to prevent nonspecific binding. Such methods are known per se to the specialist. After a subsequent in-specific coating of this type, a washing step can also be carried out. The coated sensor is incubated with the sample, this being possible, for example, by immersion in the sample or by applying a sample on the surface of the sensor. Also advantageous is an embodiment in which the surface of the sensor is shaped so that it can be measured in the throughput. It is easily understandable to the specialist what form the respective sensor should have depending on its use. By means of the reaction of the analyte with the participant in the specific connection, the magnitude of the measurement determined by the electronic switching circuit, for example the resonance frequency, is displaced. A part.r: r >; the variation of the magnitude of the measurement, can ciea'-c; The amount of bound analyte is measured, for example by comparison with a reference curve. The arrangement is also suitable for calibrating directly in units of mass. To determine the variation of the magnitude of the measurement, for example, a reference electrode that is not coated with the participant in the specific joint can be used. Advantageously, after completion of the incubation with the sample, another washing step is also carried out, the incubation with the sample can be carried out in a manner between 1 and 100 min, particularly advantageously between 5 and 60 min. very particularly advantageous form between 13 and 30 min. The regeneration can be carried out as described in DE 44 36 910. In this case, in 1: use of noble metals, preferably gold, certain reducing or oxidizing agents, such as, for example, sodium borohydride, are used as regeneration phase for the regeneration. , tetrabutylammonium hydroxide, with or without the addition of detergents. The following exemplary embodiment serves for clarification, not for the limitation of the invention. Example Quantitative determination of human IgE Support: Piezoelectric crystal of the firm Sensotec, coated with gold, set in a Teflon ring (external diameter, 36 mm). Diameter of the gold surface: 9 mm. Gold surface: 14 mm2. Coating: 50 μl of a polyclonal antibody (rabbit) against human IgE is applied to the sensor. The concentration of the antibody is 5 μg / ml. The solution also contains 75 mM Na phosphate, 75 mM NaCl, 100 g / 1 Na2? 04. The pH value is 6, 0. The antibody solution is left for 1 hour at 37 ° C or overnight at room temperature. Washing step: The supernatant is removed and the sensor is rinsed 5 times in each case with 250 μl of washing buffer. The washing buffer is composed of a solution of 50 mM tris (hydroxymethyl) aminoethane (TRIS) and 50 M citric acid, pH 7.4. Posterior lining: 50 μl of inactivated peroxidase (POD) is applied to the sensor. The POD concentration amounts to] g / 1. The solution also contains 75 mM Na phosphate, 75 mM NaCl, 10] g / 1 Na2SO4. The pH value is 6.0. The solution is left for 1 hour at 37 ° C or overnight at room temperature. Washing step: The supernatant is removed and the sensor is rinsed 5 times in each case with 250 μl of washing buffer. The washing buffer is composed of a solution of 50 mM tris (hydroxymethyl) amino-ethane (TRIS) and 50 mM citric acid, pH 4. 4. Incubation of the sample: 50 μl of human serum containing 50 μM is added to the sensor. defined amounts of IgE and incubated at 37 c for 30 min Wash step: The supernatant is removed and the sensor is rinsed 5 times in each case with 250 μl of wash buffer (5 mM Na phosphate, 85 mM NaCl, 1 g / 1 Tween 20, 0.5 g / 1 phenol, pH 6.5).
Regeneration of the solid phase: 250 μl of a 20% (wt%) solution of tetrabutylammonium hydroxide are applied to the sensor and incubated at 37 aC for 1 hour. Washing stage: After removal of the supernatant, the sensor is rinsedtimes with deionized water. 2nd regeneration: 250 μl of a 1% solution (% by weight) e * is incubated on the sensor for 15 minutes in the third environment. ? BH4. The solution also contains 2-cyclohexaic acid. ir.ce: anosulphonic (CHES) 50 mM. The pH is 10.0. Washing step: After removal of the supernatant rinse the sensor 3 times with deionized water and 3 times with a phosphate buffered sodium chloride solution (pH 7.2). Results: * 1. Determination with 100 IU / ml of human IgE = 329 Ua "2. Determination with 100 IU / ml of human IgE = 576 Ua 3. Determination with 100 IU / ml of human IgE = -23 t ^ Determination with 0 IU / ml of human IgE = 19 Ua determination with 100 IU / ml of human IgE = "or" 'Ja Determination with 100 IU / ml of human IgE (control = coating antibody inespcJ i:: -o) = 14 Ua Mean values of n = 2. Arbitrary units.

Claims (9)

2. The process according to claim 1, wherein the solid phase is coated with a noble metal, preferably gold. The method according to one of claims 1-2, wherein the first participant in the binding is an in-immunoglobulin or a fragment of in unoglobulin. Method according to at least one of claims 1-3, in which after the reaction the solid phase is regenerated by separating the first participant in the specific connection from said solid phase by means of a reagent. The method according to claim 4, wherein the reagent contains a reducing agent. 6. The method according to claim 4, wherein the reagent contains an oxidizing agent. 7. The process according to claim 4, wherein the reagent contains NaBH4. 8. The process according to claim 4, wherein the reagent contains tetrabutylammonium hydroxide. 9. Use of a regenerable solid phase of a noble metal in a process according to claim 1.
MX9606584A1995-12-271996-12-18Mass-sensitive biosensors.MX9606584A (en)

Applications Claiming Priority (2)

Application NumberPriority DateFiling DateTitle
DE19548376ADE19548376A1 (en)1995-12-271995-12-27 Mass sensitive biosensors
DE19548376.61995-12-27

Publications (2)

Publication NumberPublication Date
MXPA96006584Atrue MXPA96006584A (en)1997-06-01
MX9606584A MX9606584A (en)1997-06-28

Family

ID=7781176

Family Applications (1)

Application NumberTitlePriority DateFiling Date
MX9606584AMX9606584A (en)1995-12-271996-12-18Mass-sensitive biosensors.

Country Status (9)

CountryLink
US (1)US6087187A (en)
EP (1)EP0781999B1 (en)
JP (1)JP3848416B2 (en)
AT (1)ATE206522T1 (en)
AU (1)AU7549896A (en)
CA (1)CA2193318C (en)
DE (2)DE19548376A1 (en)
ES (1)ES2164822T3 (en)
MX (1)MX9606584A (en)

Families Citing this family (14)

* Cited by examiner, † Cited by third party
Publication numberPriority datePublication dateAssigneeTitle
US6289286B1 (en)1998-05-292001-09-11Biacore AbSurface regeneration of biosensors and characterization of biomolecules associated therewith
SE512994C2 (en)*1998-09-242000-06-12Biosensor Applic Sweden Ab Biosensor cell device and its use
SG93209A1 (en)*1999-07-052002-12-17Inst Of Molecular AgrobiologyA novel immuno-diagnostic test method for veterinary disease
JP2005504260A (en)*2000-08-092005-02-10カリフォルニア インスティテュート オブ テクノロジー Active NEMS array for biochemical analysis
EP1322951A2 (en)*2000-09-202003-07-02Molecular ReflectionsMicrofabricated ultrasound array for use as resonant sensors
WO2004082363A2 (en)*2003-03-172004-09-30Michael NerenbergSensor assembly and methods of making and using same
US7888134B2 (en)2003-06-052011-02-15Oakland UniversityImmunosensors: scFv-linker design for surface immobilization
US7464580B2 (en)*2005-09-262008-12-16Oakland UniversityIonic liquid high temperature gas sensors
US7886577B2 (en)2006-03-302011-02-15Oakland UniversityDevices with surface bound ionic liquids and method of use thereof
US8375768B2 (en)*2006-03-302013-02-19Oakland UniversityIonic liquid thin layer sensor for electrochemical and/or piezoelectric measurements
US8088596B2 (en)*2006-10-102012-01-03Oakland UniversityMethod of microorganism detection using carbohydrate and lectin recognition
US20100238035A1 (en)*2009-03-192010-09-23Tangidyne CorporationDetection device and method for detecting analyte
KR101109082B1 (en)*2010-03-162012-01-31(주)나노스토리지 Reusable Biochips and How to Use Them
US8409875B2 (en)2010-10-202013-04-02Rapid Diagnostek, Inc.Measurement of binding kinetics with a resonating sensor

Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication numberPriority datePublication dateAssigneeTitle
US4236893A (en)1979-04-091980-12-02Minnesota Mining And Manufacturing CompanyMethod for the assay of classes of antigen-specific antibodies
US4735906A (en)1984-11-281988-04-05Texas A&M UniversitySensor having piezoelectric crystal for microgravimetric immunoassays
DE3920052A1 (en)1989-06-201991-01-10Peter Dipl Ing BergInertial mass measuring system deriving physical characteristics - uses vibrating oscillator working with higher and/or variable damping e.g. in liq.
US5314830A (en)*1992-10-301994-05-24University Of New MexicoImmobilized hydrophobically-modified antibodies
DE4436910A1 (en)1994-10-151996-04-18Behringwerke Ag Regenerable solid phase for carrying out specific binding reactions

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