TY - JOUR A1 - Waiblinger, H. U. A1 - Bartsch, D. A1 - Brockmeyer, J. A1 - Bruenen-Nieweler, C. A1 - Busch, U. A1 - Haase, I. A1 - Hahn, A. A1 - Haarmann, M. A1 - Hauser, W. A1 - Huber, I. A1 - Jany, K. D. A1 - Kirmse, N. A1 - Lindeke, S. A1 - Neumann, K. A1 - Naumann, H. A1 - Paschke, A. A1 - Pietsch, K. A1 - Pöpping, B. A1 - Reiting, R. A1 - Schroeder, U. A1 - Schwägele, F. A1 - Weller, Michael G. A1 - Zagon, J. T1 - Methods of differentiating animal species in food - Status quo N2 - In the field of animal species differentiation, work on standardizing methods has been intensified in Germany in recent years, not least due to the horsemeat scandal in 2013. Even though there are now hardly ever any positive findings anymore in examinations to detect horse adulterations in foods such as lasagne, animal species differentiation altogether ranks high in detecting adulteration of foods. This article, therefore, summarises the current status of analytical techniques used in Germany with standardization at German level. It has been established by the working group "Biochemical and Molecular Biological Analytics" of the Lebensmittelchemische Gesellschaft (Food Chemistry Society within the German Chemical Society) with support of experts in the working group “Molecular biology techniques for differentiating plant and animal species" (§64 of the German Food and Feed Code - LFGB) and the "Immunology and molecular biology" task force of the food hygiene and food of animal origin working group (ALTS), both from Germany. KW - Animal species differentiation KW - Fish species KW - PCR KW - ELISA KW - LC-MS/MS PY - 2017 IS - 3 SP - 29 EP - 36 PB - Deutscher Fachverlag GmbH CY - Frankfurt am Main AN - OPUS4-43485 LA - mul AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Abbas, Ioana M. A1 - Vranic, M. A1 - Hoffmann, Holger A1 - El-Khatib, Ahmed H. A1 - Montes-Bayón, M. A1 - Möller, H. M. A1 - Weller, Michael G. T1 - Investigations of the copper peptide hepcidin-25 by LC-MS/MS and NMR (+) N2 - Hepcidin-25 was identified as the main iron regulator in the human body, and it by binds to the sole iron-exporter ferroportin. Studies showed that the N-terminus of hepcidin is responsible for this interaction, the same N-terminus that encompasses a small copper(II)-binding site known as the ATCUN (amino-terminal Cu(II)- and Ni(II)-binding) motif. Interestingly, this copper-binding property is largely ignored in most papers dealing with hepcidin-25. In this context, detailed investigations of the complex formed between hepcidin-25 and copper could reveal insight into its biological role. The present work focuses on metal-bound hepcidin-25 that can be considered the biologically active form. The first part is devoted to the reversed-phase chromatographic separation of copper-bound and copper-free hepcidin-25 achieved by applying basic mobile phases containing 0.1% ammonia. Further, mass spectrometry (tandem mass spectrometry (MS/MS), high-resolution mass spectrometry HRMS)) and nuclear magnetic resonance (NMR) spectroscopy were employed to characterize the copper-peptide. Lastly, a three-dimensional (3D)model of hepcidin-25with bound copper(II) is presented. The identification of metal complexes and potential isoforms and isomers, from which the latter usually are left undetected by mass spectrometry, led to the conclusion that complementary analytical methods are needed to characterize a peptide calibrant or reference material comprehensively. Quantitative nuclear magnetic resonance (qNMR), inductively-coupled plasma mass spectrometry (ICP-MS), ion-mobility spectrometry (IMS) and chiral amino acid analysis (AAA) should be considered among others. KW - Metalloprotein KW - Peptide KW - Chromatography KW - High pH KW - Mobile phase KW - Metrology KW - Purity KW - Reference material KW - ATCUN KW - Copper KW - Nickel PY - 2018 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-457796 UR - http://www.mdpi.com/1422-0067/19/8/2271 DO - https://doi.org/10.3390/ijms19082271 SN - 1422-0067 VL - 19 IS - 8 SP - 2271, 1 EP - 16 PB - MDPI CY - Basel AN - OPUS4-45779 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Weller, Michael G. T1 - The mystery of homochirality on earth N2 - Homochirality is an obvious feature of life on Earth. On the other hand, extraterrestrial samples contain largely racemic compounds. The same is true for any common organic synthesis. Therefore, it has been a perplexing puzzle for decades how these racemates could have formed enantiomerically enriched fractions as a basis for the origin of homochiral life forms. Numerous hypotheses have been put forward as to how preferentially homochiral molecules could have formed and accumulated on Earth. In this article, it is shown that homochirality of the abiotic organic pool at the time of formation of the first self-replicating molecules is not necessary and not even probable. It is proposed to abandon the notion of a molecular ensemble and to focus on the level of individual molecules. Although the formation of the first self-replicating, most likely homochiral molecule, is a seemingly improbable event, on a closer look, it is almost inevitable that some homochiral molecules have formed simply on a statistical basis. In this case, the non-selective leap to homochirality would be one of the first steps in chemical evolution directly out of a racemic “ocean”. Moreover, most studies focus on the chirality of the primordial monomers with respect to an asymmetric carbon atom. However, any polymer with a minimal size that allows folding to a secondary structure would spontaneously lead to asymmetric higher structures (conformations). Most of the functions of these polymers would be influenced by this inherently asymmetric folding. Furthermore, a concept of physical compartmentalization based on rock nanopores in analogy to nanocavities of digital immunoassays is introduced to suggest that complex cell walls or membranes were also not required for the first steps of chemical evolution. To summarize, simple and universal mechanisms may have led to homochiral self-replicating systems in the context of chemical evolution. A homochiral monomer pool is deemed unnecessary and probably never existed on primordial Earth. N2 - Homochiralität ist ein offensichtliches Merkmal des Lebens auf der Erde. Andererseits enthalten extraterrestrische Proben überwiegend racemische Verbindungen. Dasselbe gilt für jede gängige organische Synthese. Daher war es jahrzehntelang ein Rätsel, wie diese Racemate enantiomeren-angereicherte Fraktionen als Grundlage für den Ursprung homochiraler Lebensformen bilden konnten. Zahlreiche Hypothesen wurden aufgestellt, wie sich bevorzugt homochirale Moleküle auf der Erde gebildet und angereichert haben könnten. In diesem Artikel wird gezeigt, dass Homochiralität des abiotischen organischen Pools zum Zeitpunkt der Bildung der ersten selbstreplizierenden Moleküle nicht notwendig und nicht einmal wahrscheinlich ist. Es wird vorgeschlagen, die Vorstellung eines molekularen Ensembles aufzugeben und sich auf die Ebene der einzelnen Moleküle zu konzentrieren. Obwohl die Bildung des ersten selbstreplizierenden, höchstwahrscheinlich homochiralen Moleküls ein scheinbar unwahrscheinliches Ereignis ist, ist es bei näherer Betrachtung fast unvermeidlich, dass sich einige homochirale Moleküle einfach auf statistischer Basis gebildet haben. In diesem Fall wäre der nichtselektive Sprung zur Homochiralität einer der ersten Schritte der chemischen Evolution direkt aus einem racemischen "Ozean". Darüber hinaus konzentrieren sich die meisten Studien auf die Chiralität der ursprünglichen Monomere in Bezug auf ein asymmetrisches Kohlenstoffatom. Jedes Polymer mit einer Mindestgröße, die eine Faltung zu einer Sekundärstruktur erlaubt, würde jedoch spontan zu asymmetrischen höheren Strukturen (Konformationen) führen. Die meisten Funktionen dieser Polymere würden durch diese inhärent asymmetrische Faltung beeinflusst. Darüber hinaus wird ein Konzept der physikalischen Kompartimentierung auf der Basis von Gesteinsnanoporen in Analogie zu den Nanokavitäten digitaler Immunoassays vorgestellt, das darauf hindeutet, dass auch für die ersten Schritte der chemischen Evolution keine komplexen Zellwände oder Membranen notwendig waren. Zusammenfassend lässt sich sagen, dass einfache und universelle Mechanismen zu homochiralen selbstreplizierenden Systemen im Rahmen der chemischen Evolution geführt haben könnten. Ein homochiraler Monomerpool wird als unnötig angesehen, welcher auf der Urerde wahrscheinlich nie existiert hat. KW - Chemical evolution KW - Enantiomeric excess ee KW - Chirality KW - Racemate KW - Folding chirality KW - Self-assembly KW - self-replication KW - Single molecule KW - Prebiotic chemistry KW - Protein folding KW - Peptide folding KW - Proteinoid KW - Conformation KW - Segregation KW - Compartmentalization KW - Digital immunoassay KW - Porous rock KW - Miller and Urey KW - Primordial soup KW - Murchison meteorite KW - Micrometeorites KW - Tholins PY - 2024 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-598349 DO - https://doi.org/10.3390/life14030341 SN - 2075-1729 VL - 14 IS - 3 SP - 1 EP - 13 PB - MDPI CY - Basel AN - OPUS4-59834 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Bernevic, Bogdan A1 - El-Khatib, Ahmed H. A1 - Jakubowski, Norbert A1 - Weller, Michael G. T1 - Online immunocapture ICP‑MS for the determination of the metalloprotein ceruloplasmin in human serum N2 - The human copper-protein ceruloplasmin (Cp) is the major copper-containing protein in the human body. The accurate determination of Cp is mandatory for the reliable diagnosis of several diseases. However, the analysis of Cp has proven to be difficult. The aim of our work was a proof of concept for the determination of a metalloprotein-based on online immunocapture ICP-MS. The immuno-affinity step is responsible for the enrichment and isolation of the analyte from serum, whereas the compound-independent quantitation with ICP-MS delivers the sensitivity, precision, and large dynamic range. Off-line ELISA (enzyme-linked immunosorbent assay) was used in parallel to confirm the elution profile of the analyte with a structure-selective method. The total protein elution was observed with the 32S mass trace. The ICP-MS signals were normalized on a 59Co signal. The human copper-protein Cp could be selectively determined. This was shown with pure Cp and with a sample of human serum. The good correlation with off-line ELISA shows that Cp could be captured and eluted selectively from the anti-Cp affinity column and subsequently determined by the copper signal of ICP-MS. KW - ELISA KW - Affinity chromatography KW - Affinity extraction KW - IgY KW - Chicken antibodies KW - Immunoaffinity extraction KW - Copper KW - Diagnostics PY - 2018 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-446157 UR - https://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-018-3324-7 UR - https://static-content.springer.com/esm/art%3A10.1186%2Fs13104-018-3324-7/MediaObjects/13104_2018_3324_MOESM1_ESM.pdf UR - https://static-content.springer.com/esm/art%3A10.1186%2Fs13104-018-3324-7/MediaObjects/13104_2018_3324_MOESM2_ESM.pdf DO - https://doi.org/10.1186/s13104-018-3324-7 SN - 1756-0500 VL - 11 IS - 1 SP - Article 213, 1 EP - 5 PB - Springer Nature CY - Heidelberg AN - OPUS4-44615 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Paul, Martin A1 - Tscheuschner, Georg A1 - Herrmann, Stefan A1 - Weller, Michael G. T1 - Fast Detection of 2,4,6-Trinitrotoluene (TNT) at ppt Level by a Laser-Induced Immunofluorometric Biosensor N2 - 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. KW - Airport KW - Aviation KW - Bombs KW - Terrorism KW - Biosensing KW - Continuous Sensor KW - High-Speed KW - Ultrasensitive PY - 2020 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-511245 DO - https://doi.org/10.3390/bios10080089 VL - 10 IS - 8 SP - 89 PB - MDPI CY - Basel AN - OPUS4-51124 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Liu, F. A1 - Reinmuth-Selzle, K. A1 - Lai, S. A1 - Weller, Michael G. A1 - Pöschl, U. A1 - Kampf, C. J. T1 - Simultaneous determination of nitrated and oligomerized proteins by size exclusion high-performance liquid chromatography coupled to photodiode array detection N2 - Chemical modifications such as nitration and cross-linking may enhance the allergenic potential of proteins. The kinetics and mechanisms of the underlying chemical processes, however, are not yet well understood. Here, we present a size-exclusion chromatography/spectrophotometry method (SEC-HPLC-DAD) that allows a simultaneous detection of mono-, di-, tri-, and higher protein oligomers, as well as their individual nitration degrees (NDs). The ND results of proteins from this new method agree well with the results from an alternative well-established method, for the analysis of tetranitromethane (TNM)- and nitrogen dioxide and ozone (NO2/O3)-nitrated protein samples. Importantly, the NDs for individual oligomer fractions can be obtained from the new method, and also, we provide a proof of principle for the calculation of the concentrations for individual protein oligomer fractions by their determined NDs, which will facilitate the investigation of the kinetics and mechanism for protein tyrosine nitration and cross-linking. KW - Size exclusion chromatography KW - HPLC-DAD KW - Protein nitration degree KW - Protein oligomer analysis KW - Nitrotyrosine KW - Dimer KW - Trimer KW - Oligomer KW - Protein KW - Tetranitromethane KW - BSA KW - Albumin KW - Air pollution KW - Nitrogen oxides PY - 2017 UR - http://www.sciencedirect.com/science/article/pii/S0021967317303795 DO - https://doi.org/10.1016/j.chroma.2017.03.015 SN - 0021-9673 VL - 1495 SP - 76 EP - 82 PB - Elsevier B.V. CY - Amsterdam AN - OPUS4-40304 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Stolper, P. A1 - Fabel, S. A1 - Weller, Michael G. A1 - Knopp, D. A1 - Niessner, R. T1 - Whole-cell luminescence-based flow-through biodetector for toxicity testing N2 - A new type of biodetector was designed based on a bioluminescence test with the bacterium Vibrio fischeri performed in a liquid continuous flow-through system. Here we describe the modification of a commercial tube luminescence detector to work in the flow mode by building a new flow cell holder and a new case including “top cover” to connect the flow cell with the waste and the incubation capillary in a light-proof manner. As different samples were injected successively it was necessary to keep the individual peaks separated. This was done using an air-segmented flow in the reaction coil. To afford fast screening, the incubation time of the sample and the Vibrio fischeri, which equaled the dead time of the detection system, was set at 5.6 min. Rapid monitoring of toxic substances is achieved by using 20 µL of sample and flow-rates of 110–150 µL min-1. As a proof-of-principle, we show results for the detection of five selected di-, tri- and tetrachlorophenols at different concentrations varying from 1 to 200 mg L-1. Calculation of inhibition rates and EC50 values were performed and compared with corresponding values from the DIN EN ISO 11348-2 microplate format. Compared with the latter, the inhibition rates obtained with our flow-through biodetector for the compounds tested were generally about twofold lower, but importantly, a much faster detection is possible. KW - Biosensor KW - Air-segmented flow KW - Vibrio fischeri KW - Bioluminescence KW - Toxicity test PY - 2008 DO - https://doi.org/10.1007/s00216-007-1770-5 SN - 1618-2642 SN - 1618-2650 VL - 390 IS - 4 SP - 1181 EP - 1187 PB - Springer CY - Berlin AN - OPUS4-17713 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Schwarz, Gunnar A1 - Beck, S. A1 - Weller, Michael G. A1 - Linscheid, M.W. T1 - MeCAT - new iodoacetamide reagents for metal labeling of proteins and peptides N2 - Besides protein identification via mass spectrometric methods, protein and peptide quantification has become more and more important in order to tackle biological questions. Methods like differential gel electrophoresis or enzyme-linked immunosorbent assays have been used to assess protein concentrations, while stable isotope labeling methods are also well established in quantitative proteomics. Recently, we developed metalcoded affinity tagging (MeCAT) as an alternative for accurate and sensitive quantification of peptides and proteins. In addition to absolute quantification via inductively coupled plasma mass spectrometry, MeCAT also enables sequence analysis via electrospray ionization tandem mass spectrometry. In the current study, we developed a new labeling approach utilizing an iodoacetamide MeCAT reagent (MeCAT-IA). The MeCAT-IA approach shows distinct advantages over the previously used MeCAT with maleinimide reactivity such as higher labelling efficiency and the lack of diastereomer formation during labeling. Here, we present a careful characterization of this new method focusing on the labeling process, which yields complete tagging with an excess of reagent of 1.6 to 1, less complex chromatographic behavior, and fragmentation characteristics of the tagged peptides using the iodoacetamide MeCAT reagent. KW - Quantitative proteomics KW - Mass spectrometry KW - Metal labeling KW - Stable isotope labeling KW - Lanthanide DOTA KW - Metall-Markierung KW - Reagenzien KW - Protein-Quantifizierung KW - Lanthaniden KW - Multiplexing PY - 2011 DO - https://doi.org/10.1007/s00216-011-5189-7 SN - 1618-2642 SN - 1618-2650 VL - 401 IS - 4 SP - 1203 EP - 1209 PB - Springer CY - Berlin AN - OPUS4-23949 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Steglich, P. A1 - Bondarenko, S. A1 - Mai, C. A1 - Paul, Martin A1 - Weller, Michael G. A1 - Mai, A. T1 - CMOS-Compatible Silicon Photonic Sensor for Refractive Index Sensing Using Local Back-Side Release N2 - 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. KW - Photonic biosensor KW - Lab-on-a-chip KW - Ring resonator KW - Resonance wavelength shift KW - PIC technology KW - Back-side integration PY - 2020 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-517139 DO - https://doi.org/10.1109/LPT.2020.3019114 VL - 32 IS - 19 SP - 1241 EP - 1244 PB - IEEE AN - OPUS4-51713 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER - TY - JOUR A1 - Resch-Genger, Ute A1 - Meermann, Björn A1 - Koch, Matthias A1 - Weller, Michael G. T1 - Editorial: Analytical methods and applications in materials and life sciences N2 - Current trends in materials and life sciences are flanked by the need to push detection limits to single molecules or single cells, enable the characterization of increasingly complex matrices or sophisticated nanostructures, speed up the time of analysis, reduce instrument complexity and costs, and improve the reliability of data. This requires suitable analytical tools such as spectroscopic, separation and imaging techniques, mass spectrometry, and hyphenated techniques as well as sensors and their adaptation to application-specific challenges in the environmental, food, consumer product, health sector, nanotechnology, and bioanalysis. Increasing concerns about health threatening known or emerging pollutants in drinking water, consumer products, and food and about the safety of nanomaterials led to a new awareness of the importance of analytical sciences. Another important driver in this direction is the increasing demand by legislation, particularly in view of the 17 sustainable development goals by the United Nations addressing clean energy, industry, and innovation, sustainable cities, clean water, and responsible consumption and production. In this respect, also the development of analytical methods that enable the characterization of material flows in production processes and support recycling concepts of precious raw materials becomes more and more relevant. In the future, this will provide the basis for greener production in the chemical industry utilizing recycled or sustainable starting materials. This makes analytical chemistry an essential player in terms of the circular economy helping to increase the sustainability of production processes. In the life sciences sector, products based on proteins, such as therapeutic and diagnostic antibodies, increase in importance. These increasingly biotechnologically produced functional biomolecules pose a high level of complexity of matrix and structural features that can be met only by highly advanced methods for separation, characterization, and detection. In addition, metrological traceability and target definition are still significant challenges for the future, particularly in the life sciences. However, innovative reference materials as required for the health and food sector and the characterization of advanced materials can only be developed when suitable analytical protocols are available. The so-called reproducibility crisis in sciences underlines the importance of improved measures of quality control for all kinds of measurements and material characterization. This calls for thorough method validation concepts, suitable reference materials, and regular interlaboratory comparisons of measurements as well as better training of scientists in analytical sciences. The important contribution of analytical sciences to these developments is highlighted by a broad collection of research papers, trend articles, and critical reviews from these different application fields. Special emphasis is dedicated to often-overlooked quality assurance and reference materials. T2 - 150 years BAM: Science with impact CY - Berlin, Germany DA - 01.01.2021 KW - Analysis KW - Life sciences KW - Analytical sciences KW - Quality assurance KW - Reference material KW - Fluorescence KW - Nanoparticle KW - Sensor KW - Material sciences KW - Pollutant KW - Environment KW - Method KW - Limit of detection KW - 150th anniversary KW - ABC KW - BAM KW - Collection KW - Editorial KW - Special issue KW - Bundesanstalt für Materialforschung und -prüfung KW - Jahrestag PY - 2022 UR - https://nbn-resolving.org/urn:nbn:de:kobv:b43-550720 DO - https://doi.org/10.1007/s00216-022-04082-8 SN - 1618-2642 SN - 1618-2650 VL - 414 IS - Topical collection: Analytical methods and applications in the materials and life sciences SP - 4267 EP - 4268 PB - Springer CY - Berlin AN - OPUS4-55072 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER -