Demonstration and characterization of biomolecular enrichment on microfluidic aptamer-functionalized surfaces

This paper demonstrates and systematically characterizes the enrichment of biomolecular compounds using aptamer-functionalized surfaces within a microfluidic device. The device consists of a microchamber packed with aptamer-functionalized microbeads and integrated with a microheater and temperature sensor to enable thermally controlled binding and release of biomolecules by the aptamer. We first present an equilibrium binding-based analytical model to understand the enrichment process. The characteristics of the aptamer-analyte binding and enrichment are then experimentally studied, using adenosine monophosphate (AMP) and a specific RNA aptamer as a model system. The temporal process of AMP binding to the aptamer is found to be primarily determined by the aptamer-AMP binding kinetics. The temporal process of aptamer-AMP dissociation at varying temperatures is also obtained and observed to occur relatively rapidly (<2 s). The specificity of the enrichment is next confirmed by performing selective enrichment of AMP from a sample containing biomolecular impurities. Finally, we investigate the enrichment of AMP by either discrete or continuous introduction of a dilute sample into the microchamber, demonstrating enrichment factors ranging from 566 to 686×, which agree with predictions of the analytical model.     

Subunit‐Specific Labeling of Ubiquitin Chains by Using Sortase: Insights into the Selectivity of Deubiquitinases

Information embedded in different ubiquitin chains is transduced by proteins with ubiquitin‐binding domains (UBDs) and erased by a set of hydrolytic enzymes referred to as deubiquitinases (DUBs). Understanding the selectivity of UBDs and DUBs is necessary for decoding the functions of different ubiquitin chains. Critical to these efforts is the access to chemically defined ubiquitin chains bearing site‐specific fluorescent labels. One approach toward constructing such molecules involves peptide ligation by sortase (SrtA), a bacterial transpeptidase responsible for covalently attaching cell surface proteins to the cell wall. Here, we demonstrate the utility of SrtA in modifying individual subunits of ubiquitin chains. Using ubiquitin derivatives in which an N‐terminal glycine is unveiled after protease‐mediated digestion, we synthesized ubiquitin dimers, trimers, and tetramers with different isopeptide linkages. SrtA was then used in combination with fluorescent depsipeptide substrates to effect the modification of each subunit in a chain. By constructing branched ubiquitin chains with individual subunits tagged with a fluorophore, we provide evidence that the ubiquitin‐specific protease USP15 prefers ubiquitin trimers but has little preference for a particular isopeptide linkage. Our results emphasize the importance of subunit‐specific labeling of ubiquitin chains when studying how DUBs process these chains.     

A novel hybrid model of Bagging-based Naïve Bayes Trees for landslide susceptibility assessment

Bulletin of Engineering Geology and the Environment - Landslide susceptibility assessment was performed using the novel hybrid model Bagging-based Naïve Bayes Trees (BAGNBT) at Mu Cang Chai...     

Highly sensitive electrochemical sensor based on zirconium oxide-decorated gold nanoflakes nanocomposite 2,4-dichlorophenol detection

Journal of Applied Electrochemistry - In this study, a sensitive and selective electrochemical sensor based on a zirconia oxide-decorated gold nanoflake nanocomposite-modified glassy carbon...     

Hidden Relationships between N-Glycosylation and Disulfide Bonds in Individual Proteins

N-Glycosylation (NG) and disulfide bonds (DBs) are two prevalent co/post-translational modifications (PTMs) that are often conserved and coexist in membrane and secreted proteins involved in a large number of diseases. Both in the past and in recent times, the enzymes and chaperones regulating these PTMs have been constantly discovered to directly interact with each other or colocalize in the ER. However, beyond a few model proteins, how such cooperation affects N-glycan modification and disulfide bonding at selective sites in individual proteins is largely unknown. Here, we reviewed the literature to discover the current status in understanding the relationships between NG and DBs in individual proteins. Our results showed that more than 2700 human proteins carry both PTMs, and fewer than 2% of them have been investigated in the associations between NG and DBs. We summarized both these proteins with the reported relationships in the two PTMs and the tools used to discover the relationships. We hope that, by exposing this largely understudied field, more investigations can be encouraged to unveil the hidden relationships of NG and DBs in the majority of membranes and secreted proteins for pathophysiological understanding and biotherapeutic development.     

A filtration model for prediction of local flux distribution and optimization of submerged hollow fiber membrane module

A filtration mathematical model was developed on the basis of complete mass balance and momentum balance for the local flux distribution prediction and optimization of submerged hollow fiber membrane module. In this model, the effect of radial permeate flow on internal flow resistance was considered through a slip parameter obtained from the local flux experiments. The effects of fiber length, inside diameter, and average operating flux on local flux distribution were investigated using this model. The predicted results were in good agreement with the experimental data obtained from literature. It was also found that the asymmetry distribution of local flux could be intensified with the increase of average operating flux and fiber length, but slowed down with the increase of fiber inside diameter. Furthermore, the simulation coupled with energy consumption analysis could efficiently predict and illustrate the relationship between fiber geometry and water production efficiency. © 2015 American Institute of Chemical Engineers AIChE J, 61: 4377–4386, 2015     

Energy‐efficient power control for uplink spectrum‐sharing heterogeneous networks

This article considers energy‐efficient power control schemes for interference management in uplink spectrum‐sharing heterogeneous networks that maximize the energy efficiency of users, protect the macro base station, and support users with QoS consideration. In the first scenario, we define the objective function as the weighted sum of the energy efficiencies and develop an efficient global optimization algorithm with global linear and local quadratic rate of convergence to solve the considered problem. To ensure fairness among individual user equipments (UEs) in terms of energy efficiency, we consider the max‐min problem, where the objective is defined as the weighted minimum of the energy efficiencies, and a fractional programming theory and the dual decomposition method are jointly used to solve the problem and investigate an iterative algorithm. As by‐products, we further discuss the global energy efficiency problem and consider near‐optimal schemes. Numerical examples are provided to demonstrate significant improvements of the proposed algorithms over existing interference management schemes.     

On the evaluation of Six Sigma projects

Most of the research on the success in implementing Six Sigma agrees upon the fact that one of the key success factors is the selection of profitable projects. This seems to be especially important for high‐risk, large‐scope and long‐term projects, as is mostly the case in the design for Six Sigma projects. The purpose of this paper is to outline Six Sigma project characteristics and to present a new model for evaluating Six Sigma projects. To design a Six Sigma project evaluation model, we utilized mathematical optimization modeling techniques and real options theory. The model allows for the quantification of not only the project's value prior to its start but also its progress and the consideration of possible decisions based on this progress. Copyright © 2009 John Wiley & Sons, Ltd.