An impedance based microfluidic sensor for evaluation of individual red blood cell solute permeability.

-In this paper, we investigate a microfluidic based sensing device for cell membrane permeability measurements in real time with applications in rapid assessment of red blood cell (RBC) quality at the individual cell level. The microfluidic chip was designed with unique abilities to line up the RBCs in the centerline of the microchannel using positive dielectrophoresis (p-DEP) forces, rapid mixing of RBCs with various media (e.g.

Effect of Chitin Nanocrystals on Crystallization and Properties of Poly(lactic acid)-Based Nanocomposites.

The crystalline phase of poly(lactic acid) (PLA) has crucial effects on its own properties and nanocomposites. In this study, the isothermal crystallization of PLA, triethyl citrate-plasticized PLA (PLA-TEC), and its nanocomposite with chitin nanocrystals (PLA-TEC-ChNC) at different temperatures and times was investigated, and the resulting properties of the materials were characterized. Both PLA and PLA-TEC showed extremely low crystallinity at isothermal temperatures of 135, 130, 125 °C and times of 5 or 15 min.

Shed EBA-175 mediates red blood cell clustering that enhances malaria parasite growth and enables immune evasion.

Erythrocyte Binding Antigen of 175 kDa (EBA-175) has a well-defined role in binding to glycophorin A (GpA) during invasion of erythrocytes. However, EBA-175 is shed post invasion and a role for this shed protein has not been defined. We show that EBA-175 shed from parasites promotes clustering of RBCs, and EBA-175-dependent clusters occur in parasite culture.

Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion.

Proteases of the malaria parasite have long been investigated as drug targets. The genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and X (PMIX and PMX) were unknown.

Kinase-associated endopeptidase 1 (Kae1) participates in an atypical ribosome-associated complex in the apicoplast of Plasmodium falciparum.

The universally conserved kinase-associated endopeptidase 1 (Kae1) protein family has established roles in N(6)-threonylcarbamoyl adenosine tRNA modification, transcriptional regulation, and telomere homeostasis. These functions are performed in complex with a conserved core of protein binding partners. Herein we describe the localization, essentiality, and protein-protein interactions for Kae1 in the human malaria parasite Plasmodium falciparum.