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Sample pretreatment is the most important procedure to remove the matrix for interfacing with mass spectrometry (MS). Additionally, for the samples with low concentration, the process of preconcentration is required before MS analysis. We have newly developed a solid-phase extraction stationary phase based on C60-fullerene covalently bound to silica for purification of biomolecules of different characteristics. Silica particles of different porosity are modified with aminopropyl linker and then covalently bound to C60-fullerenoacetic acid or C60-epoxyfullerenes. The developed materials have been successfully applied as an alternative to commercially available reversed-phase materials for solid-phase extraction. C60-fullerene silica is able to retain small and hydrophilic molecules like phosphopeptides, which can be easily lost by reversed-phase sorbents. The novel materials are applied for desalting and preconcentration of proteins and peptides, especially phosphopeptides. In addition, the C60-fullerene silica is applied for the solid-phase extraction of selected flavonoids with recoveries of approximately 99%. The recoveries are compared with the commercially available solid-phase extraction materials.

Electrochemical water splitting is economically unviable due to the sluggish kinetics of the anodically uphill oxygen evolution reaction (OER).

A simple room temperature solution‐based method for the preparation of highly porous iron(III) benzenetricarboxylate coordination polymer films on the internal surface of a macroporous polystyrene‐divinylbenzene‐methacrylic acid polymer is reported. The resulting metal‐organic polymer hybrid (MOPH) maintains a high specific micropore surface area of 389 m2 g‐1 and thermal stability above 250 °C in air. The MOPH preparation is readily adapted to a capillary column, yielding a flow‐through separation device with excellent flow permeability and modest back‐pressure. The excellent separation capability of the MOPH column is demonstrated by enriching phosphopeptides from mixtures of digested proteins. This approach to MOPH synthesis is easily implemented and likely adaptable to a wide range of coordination polymers and metal‐organic frameworks.

Photothermal therapy (PPT) is a platform to fight cancer by using multiplexed interactive plasmonic nanomaterials as probes in combination with the excellent therapeutic performance of near-infrared (NIR) light. With recent rapid developments in optics and nanotechnology, plasmonic materials have potential in cancer diagnosis and treatment, but there are some concerns regarding their clinical use. The primary concerns include the design of plasmonic nanomaterials which are taken up by the tissues, perform their function and then clear out from the body. Gold nanoparticles (Au NPs) can be developed in different morphologies and functionalized to assist the photothermal therapy in a way that they have clinical value. This review outlines the diverse Au morphologies, their distinctive characteristics, concerns and limitations to provide an idea of the requirements in the field of NIR-based therapeutics.

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A nanostructured diamond-like carbon (DLC) coated digital versatile disk (DVD) target is presented as a matrix-free sample support for application in laser desorption/ionization mass spectrometry (LDI-MS). A large number of vacancies, defects, relative sp(2) carbon content, and nanogrooves of DLC films support the LDI phenomenon. The observed absorptivity of DLC is in the range of 305-330 nm (nitrogen laser, 337 nm). The universal applicability is demonstrated through different analytes like amino acids, carbohydrates, lipids, peptides, and other metabolites. Carbohydrates and amino acids are analyzed as sodium and potassium adducts. Peptides are detectable in their protonated forms, which avoid the extra need of additives for ionization. A bovine serum albumin (BSA) digest is analyzed to demonstrate the performance for peptide mixtures, coupled with the material-enhanced laser desorption/ionization (MELDI) approach. The detection limit of the described matrix-free target is investigated to be 10 fmol/microL for [Glu(1)]-fibrinopeptide B (m/z 1570.6) and 1 fmol/microL for L-sorbose (Na(+) adduct). The device does not require any chemical functionalization in contrast to other matrix-free systems. The inertness of DLC provides longer lifetimes without any deterioration in the detection sensitivity. Broad applicability allows high performance analysis in metabolomics and peptidomics. Furthermore the DLC coated DVD (1.4 GB) sample support is used as a storage device for measured and processed data together with sampling on a single device.

Over the past couple of years, proteomics pattern analysis has emerged as an effective method for the early diagnosis of diseases such as ovarian, breast, or prostate cancer, without identification of single biomarkers. MALDI-TOF MS, for example, offers a simple approach for fast and reliable protein profiling, especially by using carrier materials with various physical and chemical properties, in combination with a MALDI matrix. This approach is referred to as materialenhanced laser desorption/ionization (MELDI). In this paper, we report the development and application of derivatized carrier materials [cellulose, silica, poly(glycidyl methacrylate/divinylbenzene) (GMA/DVB) particles, and diamond powder] for fast and direct MALDI-TOF MS protein profiling. The applicability of MELDI for rapid protein profiling was evaluated with human serum samples. These carriers, having various hydrophobicities, resulted in characteristic mass fingerprints, even if all materials were derivatized with iminodiacetic acid (IDA) to yield an immobilized metal affinity chromatography (IMAC) functionality. Our study demonstrates that analyzing complex biological samples, such as human serum, by employing different MELDI carrier materials yielded type-and size-dependent performance variation. T he quest to diagnose and identify diseases at early stages depends mainly on the accurate determination of the marker entities in the biological fluids. These marker entities are normally very low concentrated [1], and highly sensitive methods are required to bind them effectively from the biosamples and to measure them with matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) [2]. MALDI mass spectrometry, in recent times, has proven to be an authentic technique to analyze peptides and proteins [3,4]. These biomolecules out of the complex biofluids like serum are difficult to ionize and thus, bring into time of flight (TOF) because of the complexity of the sample and the suppressing nonvolatile salts [5]. The aforementioned problems are tackled by another technique introduced years ago, namely, surface-enhanced laser desorption/ionization time of flight mass spectrometry (SELDI-TOF MS), for the detection of several peptides and proteins from complex biological specimens [6 -8]. This affinity-based method utilizes selective adsorption of proteins on various chromatographic surfaces to reduce sample complexity [9,10]. Spectra generated by SELDI-TOF MS usually show limited peak and binding capacity due to the smaller surface area of the plane protein chip [11]. Limitations of SELDI are also associated with the lower mass resolution of the applied MS instrument that