Computational design of a β-peptide that targets transmembrane helices

The design of β-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of β-peptides was designed to stably insert in TM orientations in phospholipid bilayers. Their secondary structures and orientation in the phospholipid bilayer was characterized using biophysical methods. Computational methods were then devised to design a β-peptide that targeted a TM helix of the integrin α(IIb)β(3). The designed peptide (β-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.     

Synthesis of cyclopentadienyl ruthenium complexes bearing pendant chelating picolinates through an electrophilic precursor

This note reports the facile synthesis of two ruthenium cyclopentadienyl half-sandwich complexes functionalized with coordinating α-picolinates. The synthetic approach involves the (η⁵-chloromethylcyclopentadienyl)(η⁶-benzene)ruthenium(II) cation as a useful common building block for cyclopentadienyl complexes bearing anchored ligands.     

Detecting functional magnetic resonance imaging activation in white matter: Interhemispheric transfer across the corpus callosum

Background  

It is generally believed that activation in functional magnetic resonance imaging (fMRI) is restricted to gray matter. Despite this, a number of studies have reported white matter activation, particularly when the corpus callosum is targeted using interhemispheric transfer tasks. These findings suggest that fMRI signals may not be neatly confined to gray matter tissue. In the current experiment, 4 T fMRI was employed to evaluate whether it is possible to detect white matter activation. We used an interhemispheric transfer task modelled after neurological studies of callosal disconnection. It was hypothesized that white matter activation could be detected using fMRI.