1.5 Proteinanalytik
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Dokumenttyp
Schlagworte
- Magnetic resonance imaging (13)
- ELISA (10)
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- 150th anniversary (2)
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- 150th anniversary of BAM (1)
- 18HTL10 (1)
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- 280 nm (1)
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- ADAMTS4 (1)
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- Acid (1)
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- Acute myocardial infarction (1)
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- Antibody-gated indicator delivery (1)
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- Antibody-gated materials (1)
- Aorta (1)
- Aromatic amino acid analysis AAAA (1)
- Aromatic amino acid analysis aaaa (1)
- Aromatische Aminosäureanalytik (1)
- Array (1)
- Atherosclerotic plaques (1)
- Atmospheric aerosol (1)
- Augenbohne (1)
- Automated Purification (1)
- Aviation (1)
- BCA (1)
- BCA test (1)
- Back-side integration (1)
- Bacterial lysates (1)
- Basic solvent (1)
- Bead-based-assay (1)
- Benchmarking study (1)
- Benzene-1,3,5-tricarboxylic acid (1)
- Bet v 1 (1)
- Betula pendula (1)
- Binder (1)
- Binding molecule (1)
- Bio-gated hybrid materials (1)
- Biochemische Sensoren (1)
- Biochemistry (1)
- Bioconjugates (1)
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- Birch pollen allergen (1)
- Block copolymer (1)
- Blood (1)
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- Border surveillance (1)
- Borosilicate Glass (1)
- Borosilicatglas (1)
- Borosilikatglas (1)
- Bovine serum albumin (1)
- Bovine serum albumin (BSA) (1)
- Bradford (1)
- Bradford-Assay (1)
- CCMV (1)
- CMOS (1)
- CMOS camera (1)
- Cardiac troponin (1)
- CardioMet (1)
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- Cardiovascular diseases (1)
- Carrier protein (1)
- Carrier-Material (1)
- Cellulose (1)
- Ceruloplasmin (1)
- Characterization (1)
- Chelate (1)
- Chemical protein modification (1)
- Chemiluminescence (1)
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- Chicken antibodies (1)
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- Chronic kidney disease (1)
- Citation (1)
- Citizen Science (1)
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- Clinical samples (1)
- Cmos (1)
- Collagen (1)
- Collision induced dissociation (CID) (1)
- Colorchanging Particles (1)
- Column holder (1)
- Combinatorial library (1)
- Combinatorial polymer libraries (1)
- Combinatorial screening (1)
- Combustion (1)
- Commercialization (1)
- Compartmentalization (1)
- Competitive Immunoassay (1)
- Compound-independent calibration (1)
- Concentration step (1)
- Confiscation (1)
- Conformation (1)
- Conjugates (1)
- Construction (1)
- Continuous Sensor (1)
- Copper-catalyzed (1)
- Corona virus (1)
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- Covalent conjugation (1)
- Crossreactivity (1)
- Customs (1)
- Cyclisierung (1)
- Cytoplasm (1)
- DHAP (1)
- DLS (1)
- DM1 (1)
- Damage-associated molecular patterns (DAMPs) (1)
- Data analysis (1)
- De novo peptide sequencing (1)
- Deep learning-based tools (1)
- Delivery system (1)
- Dendrimer (1)
- Derivatization (1)
- Detection (1)
- Diagnostic (1)
- Diagnostic Antibodies (1)
- Diagnostic antibodies (1)
- Diclofenac (1)
- Diesel exhaust (1)
- Digestion (1)
- Digital immunoassay (1)
- Dimerization (1)
- Diode laser (1)
- Dip-stick assay (1)
- Dityrosine crosslinking (1)
- Docking (1)
- Double strands (1)
- Down Stream Processing (1)
- Downstream Processing (1)
- Drohne (1)
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- Drug (1)
- Drug search (1)
- Drug trafficking (1)
- Drug transporters (1)
- Drugs (1)
- Duftstoffe (1)
- Durchflusszytometrie (1)
- Dust sensor (1)
- Dy-654 (1)
- E. coli (1)
- ECL (1)
- EDTAD (1)
- EMPIR (1)
- EP-3533 (1)
- ESEM (1)
- ESI MS (1)
- ESMA (1)
- Editorial (1)
- Elastin (1)
- Elastin-specific contrast agent ESMA (1)
- Elastin-specific molecular agent (1)
- Element Specific Bioimaging Using Laser Ablation (1)
- Emergency (1)
- Enantiomeric excess ee (1)
- Encapsulation (1)
- Enhancement (1)
- Enrichment (1)
- Environmental pollutants (1)
- Enzyme (1)
- Epifluorescence (1)
- Epoxy (1)
- Error correction (1)
- Escherichia coli (1)
- Ethylenediaminetetraacetic acid (1)
- Etofenprox (1)
- Evanescent wave (1)
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- Experiment (1)
- Explosiven (1)
- Explosives (1)
- Explosives determination (1)
- Expression (1)
- Fab Fragment (1)
- False Positives (1)
- Festphasenextraktion (1)
- Flow cytometry (1)
- Flow injection immunoassay (1)
- Flowcell (1)
- Fluorescence label (1)
- Fluoreszenz (1)
- Formulation additives (1)
- Fragment (1)
- Functionalization (1)
- Gadolinium-based contrast agent (1)
- Gadovist (1)
- Gas Tomography (1)
- Gated hybrid material (1)
- Gated materials (1)
- Gd-DOTA (1)
- Gesteuerten Nanopartikeln (1)
- Ggadolinium (1)
- Github (1)
- Glasmonolith (1)
- Glass (1)
- Glass Support (1)
- Gold particles (1)
- Gold-Nanopartikel (1)
- Grass pollen (1)
- Größenausschlusschromatographie (1)
- HMX (1)
- Halomonas elongata (1)
- Hapten Immunoassay (1)
- Hard protein corona (1)
- Hay fever (1)
- Hazardous substances (1)
- Heart attack (1)
- Heavy chains (1)
- Hepatocellular carcinoma (1)
- Heterologous hapten (1)
- HexaHis-Tag (1)
- High pH (1)
- High-Speed (1)
- High-Speed Separations (1)
- High-throughput (1)
- Highspeed (1)
- His6 (1)
- His8 (1)
- Histidine (1)
- Hochdurchsatzscreening (1)
- Horizon 2020 (1)
- Human Plasma (1)
- Human antibodies (1)
- Human antibody (1)
- Human plasma (1)
- Human serum albumin (1)
- Hydrochloric acid (1)
- Hyperbranched polymer (1)
- IC50 (1)
- IMAC purification (1)
- IgE (1)
- IgG determination (1)
- IgY (1)
- Igg (1)
- Iinductively coupled plasma mass spectrometry (1)
- Illicit drug (1)
- Illumina (1)
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- Immunglobulin (1)
- Immunglobuline (1)
- Immunoaffinity (1)
- Immunoassays (1)
- Immunochemical response optimization (1)
- Immunoglobulin E (1)
- Immunometric assay (1)
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- Immunpräzipitation (1)
- Impact (1)
- In-vivo (1)
- Inductively Coupled Mass Spectroscopy (1)
- Inductively coupled plasma mass spectroscopy (1)
- Inductively‑coupled mass spectrometry (1)
- Inhibition (1)
- Insecticide (1)
- Internal standard (1)
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- International drug trade (1)
- Ion mobility spectrometry (1)
- Iron deficiency (1)
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- Java GUI (1)
- Kjeldahl (1)
- Klon A1.1.1 (1)
- Klon EW75C (1)
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- Korrelationsmatrix (1)
- Kreuzreaktion (1)
- LC-MS/MS peptide quantification (1)
- LC-UV absorbance (1)
- LFIA (1)
- LIF (1)
- Lab on a Chip (1)
- Lab on a chip (1)
- Lab-on-a-Chip (1)
- Lab-on-chip (1)
- Label (1)
- Ladder sequencing (1)
- Laser (1)
- Laser ablation (1)
- Laser ablation-inductively coupled plasma-mass spectrometry (1)
- Laser ablation-inductively coupled plasma-mass spectroscopy (1)
- Laser-Induced Plasma (1)
- Laser-induced fluorescence (1)
- Laser-induced plasma (1)
- Lateral flow immunoassays (1)
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- Latex particles (1)
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- MR Angiography (1)
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- Material-binding Peptides (1)
- Medicine (1)
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- Miller and Urey (1)
- Missing fragmentation sites (1)
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- Molecular marker (1)
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- Monoclonal Antibody (1)
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- NIST-mAb 8671 (1)
- NMR (1)
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Organisationseinheit der BAM
- 1 Analytische Chemie; Referenzmaterialien (125)
- 1.5 Proteinanalytik (125)
- 1.9 Chemische und optische Sensorik (16)
- 1.8 Umweltanalytik (13)
- 6 Materialchemie (11)
- 1.1 Anorganische Spurenanalytik (10)
- 6.3 Strukturanalytik (10)
- 8 Zerstörungsfreie Prüfung (7)
- 8.1 Sensorik, mess- und prüftechnische Verfahren (7)
- 1.7 Organische Spuren- und Lebensmittelanalytik (5)
Eingeladener Vortrag
- nein (9)
To investigate the imaging performance of an elastin-specific molecular magnetic resonance imaging (MRI) probe with respect to the extracellular matrix (ECM) in an experimental hepatic cancer model. Twelve rabbits with hepatic VX2 tumors were examined using 3 T MRI 14, 21, and 28 days after tumor implantation for two subsequent days (gadobutrol, day 1; elastin-specific probe, day 2). The relative enhancement (RE) of segmented tumor regions (central and margin) and the peritumoral matrix was calculated using pre-contrast and delayed-phase T1w sequences. MRI measurements were correlated to histopathology and element-specific and spatially resolved mass spectrometry (MS). Mixed-model analysis was performed to assess the performance of the elastin-specific probe. In comparison to gadobutrol, the elastin probe showed significantly stronger RE, which was pronounced in the tumor margin (day 14–28: P ≤ 0.007). In addition, the elastin probe was superior in discriminating between tumor regions (χ2(4) = 65.87; P < 0.001). MRI-based measurements of the elastin probe significantly correlated with the ex vivo elastinstain (R = .84; P <0 .001) and absolute gadolinium concentrations (ICP-MS: R = .73, P <0 .01). LA-ICP-MS imaging confirmed the colocalization of the elastin-specific probe with elastic fibers. Elastin-specific molecular MRI is superior to non-specific gadolinium-based contrast agents in imaging the ECM of hepatic tumors and the peritumoral tissue.
Background:
Molecular-MRI is a promising imaging modality for the assessment of abdominal aortic aneurysms (AAAs). Interleukin-1β (IL-1β) represents a new therapeutic tool for AAA-treatment, since pro-inflammatory cytokines are key-mediators of inflammation. This study investigates the potential of molecular-MRI to evaluate therapeutic effects of an anti-IL-1β-therapy on AAA-formation in a mouse-model.
Methods:
Osmotic-minipumps were implanted in apolipoprotein-deficient-mice (N = 27). One group (Ang-II+01BSUR group, n = 9) was infused with angiotensin-II (Ang-II) for 4 weeks and received an anti-murine IL-1β-antibody (01BSUR) 3 times. One group (Ang-II-group, n = 9) was infused with Ang-II for 4 weeks but received no treatment. Control-group (n = 9) was infused with saline and received no treatment. MR-imaging was performed using an elastin-specific gadolinium-based-probe (0.2 mmol/kg).
Results:
Mice of the Ang-II+01BSUR-group showed a lower aortic-diameter compared to mice of the Ang-II-group and control mice (p < 0.05). Using the elastin-specific-probe, a significant decrease in elastin-destruction was observed in mice of the Ang-II+01BSUR-group. In vivo MR-measurements correlated well with histopathology (y = 0.34x-13.81, R2 = 0.84, p < 0.05), ICP-MS (y = 0.02x+2.39; R2 = 0.81, p < 0.05) and LA-ICP-MS. Immunofluorescence and western-blotting confirmed a reduced IL-1β-expression.
Conclusions:
Molecular-MRI enables the early visualization and quantification of the anti-inflammatory-effects of an IL-1β-inhibitor in a mouse-model of AAAs. Responders and non-responders could be identified early after the initiation of the therapy using molecular-MRI.
CMOS-Compatible Silicon Photonic Sensor for Refractive Index Sensing Using Local Back-Side Release
(2020)
Silicon photonic sensors are promising candidates for lab-on-a-chip solutions with versatile applications and scalable production prospects using complementary metal-oxide semiconductor (CMOS) fabrication methods. However, the widespread use has been hindered because the sensing area adjoins optical and electrical components making packaging and sensor handling challenging. In this work, a local back-side release of the photonic sensor is employed, enabling a separation of the sensing area from the rest of the chip. This approach allows preserving the compatibility of photonic integrated circuits in the front-end of line and metal interconnects in the back-end of line. The sensor is based on a micro-ring resonator and is fabricated on wafer-level using a CMOS technology. We revealed a ring resonator sensitivity for homogeneous sensing of 106 nm/RIU.
Environmental pollutants like fine particulate matter can cause adverse health effects through oxidative stress and inflammation. Reactive oxygen and nitrogen species (ROS/RNS) such as peroxynitrite can chemically modify proteins, but the effects of such modifications on the immune system and human health are not well understood. In the course of inflammatory processes, the Toll-like receptor 4 (TLR4) can sense damage-associated molecular patterns (DAMPs). Here, we investigate how the TLR4 response and pro-inflammatory potential of the proteinous DAMPs α-Synuclein (α-Syn), heat shock protein 60 (HSP60), and high-mobility-group box 1 protein (HMGB1), which are relevant in neurodegenerative and cardiovascular diseases, changes upon chemical modification with peroxynitrite.
For the peroxynitrite-modified proteins, we found a strongly enhanced activation of TLR4 and the pro-inflammatory transcription factor NF-κB in stable reporter cell lines as well as increased mRNA expression and secretion of the pro-inflammatory cytokines TNF-α, IL-1β, and IL-8 in human monocytes (THP-1). This enhanced activation of innate immunity via TLR4 is mediated by covalent chemical modifications of the studied DAMPs.
Our results show that proteinous DAMPs modified by peroxynitrite more potently amplify inflammation via TLR4 activation than the native DAMPs, and provide first evidence that such modifications can directly enhance innate immune responses via a defined receptor. These findings suggest that environmental pollutants and related ROS/RNS may play a role in promoting acute and chronic inflammatory disorders by structurally modifying the body's own DAMPs. This may have important consequences for chronic neurodegenerative, cardiovascular or gastrointestinal diseases that are prevalent in modern societies, and calls for action, to improve air quality and climate in the Anthropocene.
Antibody-gated indicator delivery (gAID) systems based on mesoporous silica nano- and microparticle scaffolds are a promising class of materials for the sensitive chemical detection of small-molecule analytes in simple test formats such as lateral flow assays (LFAs) or microfluidic chips. Their architecture is reminiscent of drug delivery systems, only that reporter molecules instead of drugs are stored in the voids of a porous host particle. In addition, the pores are closed with macromolecular “caps” through a tailored “gatekeeping” recognition chemistry so that the caps are opened when an analyte has reacted with a “gatekeeper”. The subsequent uncapping leads to a release of a large number of indicator molecules, endowing the system with signal amplification features. Particular benefits of such systems are their modularity and adaptability. With the example of the immunochemical detection of type-I pyrethroids by fluorescent dye-releasing gAID systems, the influence of several tuning modes on the optimisation of such hybrid sensory materials is introduced here. In particular, different mesoporous silica supports (from nano- and microparticles to platelets and short fibres), different functionalisation routes and different loading sequences were assessed. The materials’ performances were evaluated by studying their temporal response behaviour and detection sensitivity, including the tightness of pore closure (through the amount of blank release in the absence of analyte) and the release kinetics. Our results indicate that the better the paratope-accommodating Fab region of the antibody “cap” fits into the host material's pore opening, the better the closing/opening mechanism can be controlled. Because such materials are well-suited for LFAs, performance assessment included a test-strip format besides conventional assays in suspension. In combination with dyes as indicators and smartphones for read-out, simple analytical tests for use by untrained personnel directly at a point-of-need such as an aeroplane cabin can be devised, allowing for sensitivities down to the μg kg−1 range in <5 min with case-required selectivities.
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.
Gegenwärtig ist das Interesse und der Bedarf von Proteinbindern insbesondere in der Biotechnik und Pharmaforschung sehr groß. Kombinatorische, Partikel-basierte (One-Bead-One-Compound) Peptidbibliotheken sind eine Technik, um selektiv bindende Proteine zu identifizieren. Allerdings beinhaltet das Screening dieser Peptidbibliotheken aufwendige Schritte, wie die Separation, Sequenzierung und Charakterisierung von identifizierten Bindern. In dieser Arbeit wurde ein Chip-System entwickelt, auf dem alle Schritte eines Screenings durchgeführt werden können. Dafür wurde ein Glasobjektträger mit einem magnetisch leitenden, doppelseitigen Klebeband versehen. Die Partikel der Bibliothek wurden durch ein Sieb aufgetragen. Dies führte zu einer geordneten Immobilisierung der Partikel auf dem Chip. Über 30.000 Partikel konnten so auf einem Chip immobilisiert werden. Für die Identifizierung von selektiven Protein-bindenden Peptiden wird die immobilisierte Peptidbibliothek mit einem Fluorophor-markierten Protein inkubiert, bindende Partikel mittels Fluoreszenzscan identifiziert und die Peptidsequenz direkt auf dem Chip mittels Matrix-Assisted-Laser-Desorption/Ionization-(MALDI)-Flugzeit-(TOF)-Massenspektroskopie (MS) bestimmt. Die Durchführung einer Abbruchsequenz-Methode erlaubt die eindeutige Bestimmung der Peptidsequenzen mit einer nahezu 100 % Genauigkeit. Die entwickelte Technologie wurde in einem FLAG-Peptid-Modell validiert. Bei dem Screening wurden neue anti-FLAG-Antikörper-bindende Peptide identifiziert. Anschließend wurden in einem Screening von ca. 30.000 Partikeln IgG-bindende Peptide mit mittleren mikromolaren Dissoziationskonstanten identifiziert. Für die Identifizierung stärkerer Binder wurde eine magnetische Anreicherung entwickelt, die dem Chip-Screening vorgeschaltet werden kann. Hiermit wurden aus ca. 1 Million gescreenter Partikel, Peptide mit Dissoziationskonstanten im niedrigen mikromolaren Bereich identifiziert.
The illegal use of explosives by terrorists and other criminals is an increasing issue in public spaces, such as airports, railway stations, highways, sports venues, theaters, and other large buildings. Security in these environments can be achieved by different means, including the installation of scanners and other analytical devices to detect ultra-small traces of explosives in a very short time-frame to be able to take action as early as possible to prevent the detonation of such devices. Unfortunately, an ideal explosive detection system still does not exist, which means that a compromise is needed in practice. Most detection devices lack the extreme analytical sensitivity, which is nevertheless necessary due to the low vapor pressure of nearly all explosives. In addition, the rate of false positives needs to be virtually zero, which is also very difficult to achieve. Here we present an immunosensor system based on kinetic competition, which is known to be very fast and may even overcome affinity limitation, which impairs the performance of many traditional competitive assays. This immunosensor 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. In the case of the explosive 2,4,6-trinitrotoluene (TNT), some binding sites of the antibody will be blocked, which leads to an immediate breakthrough of the labeled protein, detectable by highly sensitive laser-induced fluorescence with the help of a Peltier-cooled complementary metal-oxide-semiconductor (CMOS) camera. Liquid handling is performed with high-precision syringe pumps and chip-based mixing-devices and flow-cells. The system achieved limits of detection of 1 pM (1 ppt) of the fluorescent label and around 100 pM (20 ppt) of TNT. The total assay time is less than 8 min. A cross-reactivity test with 5000 pM solutions showed no signal by 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). This immunosensor belongs to the most sensitive and fastest detectors for TNT with no significant cross-reactivity by non-related compounds. The consumption of the labeled antibody is surprisingly low: 1 mg of the reagent would be sufficient for more than one year of continuous biosensor operation.
Phage display biopanning with Illumina next-generation sequencing (NGS) is applied to reveal insights into peptide-based adhesion domains for polypropylene (PP). One biopanning round followed by NGS selects robust PP-binding peptides that are not evident by Sanger sequencing. NGS provides a significant statistical base that enables motif analysis, statistics on positional residue depletion/enrichment, and data analysis to suppress false-positive sequences from amplification bias. The selected sequences are employed as water-based primers for PP-metal adhesion to condition PP surfaces and increase adhesive strength by 100% relative to nonprimed PP.