Clustering of Giant Unilamellar Vesicles Promoted by Covalent and Noncovalent Bonding of Functional Groups at Membrane-Embedded Peptides.

Access to clusters of cell-sized globular objects such as giant unilamellar vesicles (GUVs) is of increasing interest due to their potential applications in prototissue and cell-cell adhesion studies. Aggregations of GUVs by four different approaches were observed via covalent as well as noncovalent bond participations of functional groups at membrane embedded cholesterylpeptides using optical microscopy. Passive air oxidation of GUV-surface thiols into trans-GUV disulfide bonds promoted multivesicle aggregation.

ABO Blood Group Antigen Decorated Giant Unilamellar Vesicles Exhibit Distinct Interactions with Plasmodium falciparum Infected Red Blood Cells.

Severe malaria is considered to be the deadliest disease of this century, primarily among children in sub-Saharan Africa. It stems from infection by the virulent parasite Plasmodium falciparum. The pathogenesis of the disease is based on the rosetting phenomenon, which occurs during the life cycle of the parasite in red blood cells (RBCs) and promotes the binding of parasitized RBCs to healthy ones.

Synthesis of BODIPY-Labeled Cholesterylated Glycopeptides by Tandem Click Chemistry for Glycocalyxification of Giant Unilamellar Vesicles (GUVs).

The glycocalyx cover membrane surfaces of all living cells. These complex architectures render their interaction mechanisms on the membrane surface difficult to study. Artificial cell-sized membranes with selected and defined glycosylation patterns may serve as a minimalistic approach to systematically study cell surface glycan interactions.