1.5 Proteinanalytik
Filtern
Dokumenttyp
- Posterpräsentation (25) (entfernen)
Referierte Publikation
- nein (25) (entfernen)
Schlagworte
- Copper (4)
- Peptides (4)
- ATCUN (3)
- Antibody (3)
- Fluorescence (3)
- Metalloproteins (3)
- Biosensor (2)
- Cellulose (2)
- Combinatorial peptide library (2)
- Drone (2)
- ESI-MS (2)
- Explosive (2)
- Fusion protein (2)
- Iron disorders (2)
- Lab-on-a-chip (2)
- Nickel (2)
- Passive Smart Dust (2)
- Peptide library (2)
- Pyrethroids (2)
- RP-HPLC (2)
- SDS-PAGE (2)
- SUMO (2)
- Screening (2)
- Smart Dust (2)
- 18HTL10 (1)
- ADAMTS4 (1)
- Acid (1)
- Affinity (1)
- Affinity chromatography (1)
- Affinity enrichment (1)
- Affinity extraction (1)
- Affinity support (1)
- Affinty (1)
- Air traffic (1)
- Aluminum oxide (1)
- Ambient Desorption/Ionization (1)
- Amino acid analysis (1)
- Amplification (1)
- Antibodies (1)
- Antibody purification (1)
- Aorta (1)
- Aromatic amino acid analysis AAAA (1)
- BSA (1)
- Bead-based-assay (1)
- Bioconjugates (1)
- Biotechnology (1)
- Blood (1)
- Bovine serum albumin (1)
- CardioMet (1)
- Cardiovascular diseases (1)
- Characterization (1)
- Chromatography (1)
- Clinical samples (1)
- Clones (1)
- Colorchanging Particles (1)
- Colorimetric Sensor (1)
- Combinatorial library (1)
- Combinatorial screening (1)
- Confetti (1)
- Contrast agent (1)
- Data analysis (1)
- Database (1)
- Delivery system (1)
- Diagnostic (1)
- Diclofenac (1)
- Digestion (1)
- Downstream processing (1)
- Drohne (1)
- Drugs (1)
- ECL (1)
- EMPIR (1)
- ESEM (1)
- Flow cytometry (1)
- Fragment (1)
- Glue (1)
- Glutaraldehyde (1)
- Horizon 2020 (1)
- Human plasma (1)
- Hybrid materials (1)
- Hydrolysis (1)
- ICP-MS (1)
- Illumina (1)
- Imaging (1)
- Immunoaffinity (1)
- Immunoassay (1)
- Indicator (1)
- Kolorimetrische Sensoren (1)
- LC-MS/MS peptide quantification (1)
- Lab on a Chip (1)
- Laser-Induced Plasma (1)
- Luminol (1)
- MALDI-TOF mass spectrometry (1)
- Magnetic resonance imaging (1)
- Mass Spectrometry (1)
- Mass spectrometry (1)
- Medicine (1)
- Metalloprotein (1)
- Mobile Robotic Olfaction (1)
- Monoclonal antibodies (1)
- Monolith (1)
- NMR (1)
- OBOC (1)
- OBOC library (1)
- Online (1)
- Online fluorescence (1)
- PEG (1)
- Peroxidase (1)
- Pharmaceuticals (1)
- Phosphonic acids (1)
- Plasma (1)
- Polyglycerol (1)
- Polymer (1)
- Protein a (1)
- Protein g (1)
- Protein hydrolysis (1)
- Protein immobilization (1)
- Protein quantification (1)
- Raid test (1)
- Reductive amination (1)
- Remote Detection (1)
- Risk assessment (1)
- SAFIA (1)
- SALSA (1)
- Sanger sequencing (1)
- Sapphire (1)
- Sensor (1)
- Serum (1)
- Signal amplification (1)
- Source Localization (1)
- Synthetic peptides (1)
- TEM (1)
- TNT (1)
- Test strip (1)
- Trinitro (1)
- Trypsin (1)
- Tyrosine (1)
- Validation (1)
Organisationseinheit der BAM
- 1 Analytische Chemie; Referenzmaterialien (25)
- 1.5 Proteinanalytik (25)
- 1.9 Chemische und optische Sensorik (4)
- 8 Zerstörungsfreie Prüfung (4)
- 8.1 Sensorik, mess- und prüftechnische Verfahren (4)
- 1.8 Umweltanalytik (2)
- 6 Materialchemie (2)
- 6.3 Strukturanalytik (2)
- 1.1 Anorganische Spurenanalytik (1)
- 1.3 Instrumentelle Analytik (1)
Use/distribution of cost-effective and biocompatible pieces of cellulose paper as passive optical chemosensors and readout by the camera system.
Modification of the paper surface using various chemically sensitive dyes (indicators) provides an optically detectable reaction and conclusions about the target substances and precise location.
Communities worldwide face significant threats from Explosive Remnants of War (ERW), which endanger lives and restrict land usage. From forest fires due to ERWs or in ERW-contaminated areas (e.g., in Jüterbog, Germany) to broader global challenges (e.g., the Ukrainian conflict), the need for efficient detection and removal of these remnants, especially for humanitarian demining, is paramount. Traditional methods, like manual demining, have severe limitations in safety and efficiency. Here, we introduce an innovative solution to these challenges: “Chemosensing Smart Dust.” This technology uses chemoselective dyes that change their fluorescence properties when exposed to explosives like 2,4,6-trinitrotoluene (TNT). Fluorescence-based detection offers superior sensitivity, reduced likelihood of false positives, and enhanced accuracy of explosive detection. Drones, equipped with excitation lasers or LEDs, deploy the Chemosensing Smart Dust over areas of interest and actively detect the fluorescence changes using high-resolution cameras, offering a rapid, safe, and adaptable detection method. Beyond demining, this innovative approach has potential applications in monitoring polluted areas, homeland security, and emergency response.
Screening against ADAMTS4 reveals a specific peptide, which was turned into an MRI probe. The aneurysm in a mouse modal was visualized via MRI. A differentiation between stable and unstable aneurysm in an early state was performed. Using the probe as tool for an easy and non-invasive rupture assessment is possible.
Nonporous corundum powder was functionalized covalently with protein binders to isolate and enrich specific proteins from complex matrices.The common crosslinker glutaraldehyde was compared with a hyperbranched polyglycerol (PG) of around 10 kDa. The latter was oxidized with periodate to generate aldehyde groups that can covalently react with the amines of the surface and the amino groups from the protein via a reductive amination process. The amount of bound protein was quantified via aromatic amino acid analysis (AAAA). As a proof of concept, IgG was extracted with protein A from crude human plasma. The advantages of corundum include the very low price, extremely high physical and chemical stability, pressure resistance, favorable binding kinetics, convenient handling, and flexible application.
High demand for remote sensing of hazardous substances. Possible solution: Use of distributed, low cost, and environmentally safe particles as passive sensors that can be read out remotely
Chemical intelligence on the particle surface can be easily modified Particles enable optically quantifiable response and inference of target substances (also no maintenance or power supply required
Cardiovascular diseases are the number one cause of death worldwide and responsible for 3.9 million deaths in Europe and over 1.8 million deaths in the European Union (2017) [1]. Cardiac Troponin I (cTnI) is part of a triple protein complex and the most important biomarker for acute events such as heart attacks. Once a heart attack occurs, the blood stream within the heart is interrupted and further oxygen supply cannot be maintained. As a result, heart cells undergo apoptosis and their proteins will be released into the blood stream. Within the project CardioMet of the European Metrology Program of Research and Innovation (EMPIR) a biosensor for online-monitoring of acute myocardial infarction by detecting cTnI is being developed.
Antibodies are the most used biomolecules in analytical research. Nevertheless, the sequence and structure information of antibodies is often limited, since manufacturers keep them secret or suppliers sell them under different names. This can make it difficult to reproduce even basic experiments performed in publications as the antibodies used might not be identifiable. To overcome these problems, we developed a simple and cheap method for antibody identification by MALDI-TOF-MS fingerprinting. This technique was used to generate a library of antibody fingerprints, which enables the identification and comparison of antibodies in short time.
The antibody A.1.1.1 was labeled and found to be very sensitive and highly selective for TNT. A novel monolithic affinity column was coated with a Trinitroaniline (TNA)-BSA affinity conjugate and a custom laser induced fluorescence detector were built to allow for continuous and sensitive detection. The affinity column combined with the high sensitivity detector resulted in a limit of detection of approx. 100 pM TNT or 20 ppt TNT for offline detection and was able to detect picogram amounts within three minutes.
The mechanism of this system is based on kinetic competition. This biosensor consists of a monolithic glass column with a vast excess of immobilized hapten, which traps the fluorescently labeled antibody as long as no explosive is present. If the explosive 2,4,6-trinitrotoluene (TNT) is introduced some binding sites of the antibody will be blocked, which leads to an immediate breakthrough of the labeled protein. The fluorescence is detected by highly sensitive laser-induced fluorescence with a conventional CMOS camera. The system achieved limits of detection of approx.1 pM (1 ppt) of the fluorescent label and around 100 pM (20 ppt) of TNT. The total assay time is less than 8 minutes. A cross-reactivity test with 5000 pM solutions of pentaerythritol tetranitrate (PETN), 1,3,5-trinitroperhydro-1,3,5-triazine (RDX), and octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine (HMX) showed no cross reactivity.