ABSTRACT
It is common knowledge that the O2 evolution reaction (OER) is a crucial half-reaction in the electrolysis of water. However, it is currently difficult to create inexpensive OER electrode materials in a way that is efficient, simple, and environmentally friendly. In this research, metal oxy-hydroxides with numerous oxygen defects (M-OOHv) are created at surface of Cu foam (CF) using a unique, straightforward electro-oxidation reconstitution (ER) process. Different spectroscopic and microscopy methods are used to analyse the electrode characteristics of Al2Cu-MOF@M-OOHv-ER/CF; electrochemical measurements display a lower overpotential (η) of 366 mV @ 10 mA cm-2 and a Tafel slope of 95.2 mV dec-1 in 1.0 M KOH. X-Ray diffraction (XRD), scanning electron microscopy (SEM), and Raman studies confirm the phase transition of the metal-organic framework (MOF) to the M-OOH, which acts as the active site to boost the OER activity. Through spectroscopic and microscopic investigations, it is determined that the efficiency of bimetallic electrode materials and oxygen vacancies in the M-OOHv have an impact on the electron power density. The manufactured electrode material additionally showed good durability for 50 hours. As a result, the newly developed Al2Cu-MOF@M-OOHv-ER/CF nanomaterial has greater potential for both electrolysis of water and other energy storage equipment.
ABSTRACT
The development of new high throughput methods based on different materials with chemical modifications for protein profiling of complex mixtures leads towards biomarkers; used particularly for early diagnosis of a disease. In this work, diamond-like carbon (DLC) is developed and optimized for serum protein profiling by matrix-assisted laser/desorption ionization mass spectrometry (MALDI-MS). This study is carried out in connection with a material-based approach, termed as material-enhanced laser desorption ionization mass spectrometry. DLC is selected as carrier surface which provides large surface to volume ratio and offers high sensitivity. DLC has a dual role of working as MALDI target while acting as an interface for protein profiling by specifically binding peptides and proteins out of serum samples. Serum constituents are bound through immobilized metal ion affinity chromatography (IMAC) functionality, created through glycidyl methacrylate polymerization under ultraviolet light followed by further derivatization with iminodiacetic acid and copper ion loading. Scanning electron microscopy highlights the morphological characteristics of DLC surface. It could be demonstrated that IMAC functionalized DLC coatings represent a powerful material in trapping biomolecules for their further analysis by MALDI-MS resulting in improved sensitivity, specificity and capacity in comparison to other protein-profiling methods.