Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat.

Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection. We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose.

Impact of Amino Acids on the Isomerization of the Aluminum Tridecamer Al.

The stability of the Keggin polycation ε-Al is monitored by Al NMR and ferron colorimetric assay upon heating aluminum aqueous solutions containing different amino acids with overall positive, negative, or no charge at pH 4.2. A focus on the effect of the amino acids on the isomerization process from ε- to δ-Al is made, compared and discussed as a function of the type of organic additive.

Sweating the small stuff: Glycoproteins in human sweat and their unexplored potential for microbial adhesion.

There is increasing evidence that secretory fluids such as tears, saliva and milk play an important role in protecting the human body from infection via a washing mechanism involving glycan-mediated adhesion of potential pathogens to secretory glycoproteins. Interaction of sweat with bacteria is well established as the cause of sweat-associated malodor. However, the role of sweat glycoproteins in microbial attachment has received little, if any, research interest in the past.

Cyclodextrin polyrotaxanes as a highly modular platform for the development of imaging agents.

Selectively functionalized cyclodextrins with a bodipy fluorescent tag or Gd(3+) complex were synthetized and threaded onto a polyammonium chain to form polyrotaxanes. This modular supramolecular assembly makes an ideal platform for bimodal (fluorescent and MRI) imaging applications.

Solid-state hierarchical cyclodextrin-based supramolecular polymer constructed by primary, secondary, and tertiary azido interactions.

The crystallization of a di-azido-α-cyclodextrin revealed a polymeric self-assembly involving a variety of azido-type interactions. The crystal arrangement relies on the cooperativity of a primary azido inclusion, a secondary azido-azido interaction involving an unprecedented distribution of canonical forms, and a tertiary azido-groove interaction. The second azido group brings in a major contribution to the supramolecular structure illustrating the benefit of a difunctionalization for the generation of hierarchy.

Beta cyclodextrins bind, stabilize, and remove lipofuscin bisretinoids from retinal pigment epithelium.

Accumulation of lipofuscin bisretinoids (LBs) in the retinal pigment epithelium (RPE) is the alleged cause of retinal degeneration in genetic blinding diseases (e.g., Stargardt) and a possible etiological agent for age-related macular degeneration.

Cyclodextrins selectively modified on both rims using an O-3-debenzylative post-functionalisation, a consequence of the Sorrento meeting.

A de-O-benzylation reaction induced by I(2)-Et(3)SiH and developed by Iadonisi et al. on mono- and disaccharides was applied to per- or polybenzylated α-cyclodextrins to furnish compounds deprotected at position 3 of all sugar units. This methodology allows the straightforward post-functionalisation of the secondary rim of cyclodextrins already functionalised on their primary rim.