Low-molecular-weight human serum proteome using ultrafiltration, isoelectric focusing, and mass spectrometry

Identification of the serum proteome is a daunting analytical task due to the complex nature of the sample which has an extremely large dynamic range of protein components. This report addresses this issue by using centrifugal ultrafiltration to enrich the low-molecular-weight (LMW) serum proteome while decreasing the amount of abundant high-molecular-weight proteins. Reduction of the complex nature of the sample was achieved by fractionation of the LMW serum proteins using solution-phase isoelectric focusing (IEF). Multiple enzyme digestions are performed and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Analysis of the tandem mass spectra resulted in the identification of 262 proteins belonging to LMW serum proteome. Our results demonstrate the effectiveness of this methodology to isolate and identify LMW proteins with improved confidence in the MS data acquired. In addition, our methodology can be combined with other multidimensional chromatography techniques performed on the peptide level to increase the number of identified proteins.     

Determination of Magnesium Ascorbyl Phosphate in Cosmetic Bleaching Products Using a Disposable Screen-Printed Carbon Electrode

A preanodized screen-printed carbon electrode is used for the determination of magnesium ascorbyl phosphate in cosmetic bleaching products. The preanodization process exhibits a marked enhancement of the current response of magnesium ascorbyl phosphate at the screen-printed carbon electrode. The linear range is up to 240 (correlation coefficient = 0.999) in pH 2.0 citrate buffer with a detection limit (S/N = 3) of 0.33 μM. The electrode has the advantages of low cost and easy of handling and can be either disposable or reused since the renewal gives a good reproducible surface. Quantitative analysis was performed by the standard addition method for magnesium ascorbyl phosphate content in cosmetic products.     

Effect of vertical vibrations on a two-layer system with a deformable interface

The effect of single- and two-frequency vibrations on the behavior of a system consisting of two homogeneous viscous fluids bounded by rigid walls is analyzed. It is assumed that the system as a whole is under vertical vibrations obeying a certain law. An eigenvalue problem is obtained in order to analyze the stability of the relative equilibrium. The case of finite frequencies and arbitrary modulation amplitudes is treated along with the case of high frequencies and small modulation amplitudes. In the former case, the parametric resonance domains are examined depending on the parameters of the system. In the latter case, the high-frequency vibration is shown to create effective surface tension, thus flattening the interface, and can suppress instability when the heavy fluid is over the light one.     

Recent advances in the use of ionic liquids as solvents for protein-based materials and chemistry

Proteins are a diverse class of molecules that can act as catalysts and structural components. Interest in their interactions with ionic solvents is on the increase due to the tuneable possibilities for non-aqueous biocatalysis, improved thermostability of biomaterials, and possible roles in medicine, such as drug delivery and use as cell-growth scaffolds. We summarise here the recent examples of these exciting new aspects of protein-ionic solvent interactions, highlighting future directions.     

Terrein

The fungal metabolite terrein (alternative name: trans‐2,3‐di­hydroxy‐4‐propenyl­cyclo­pent‐4‐enone), C₈H₁₀O₃, forms monoclinic (P2₁) crystals. The mol­ecules form hydrogen‐bonded chains, with O?O distances of 2.7115 (16) and 2.8155 (15) Å.