In a two-step thermal/photoirradiation treatment under dilute conditions, the ABA block copolymer forms both BTA-based helical aggregates and UPy dimers intramolecularly.

The sequential association of the two self-assembling motifs results in single-chain folding of the polymer, affording nanometer-sized particles with a compartmentalized interior. Variable-temperature NMR studies showed that the BTA and UPy self-assembly steps take place orthogonally (i.e., without mutual interference) in dilute solution. In addition, monitoring of the intramolecular self-assembly of BTA moieties into helical aggregates by circular dichroism spectroscopy showed Nepicastat cost that the stability of the aggregates is almost independent of UPy dimerization. Size-exclusion chromatography (SEC) and small-angle X-ray scattering analysis provided evidence of significant

reductions in the hydrodynamic volume and radius of gyration, respectively, 5-Fluoracil ic50 after photoinduced deprotection of the UPy groups; a 30-60% reduction in the size of the polymer chains was observed using SEC in CHCl3. Molecular imaging by atomic force microscopy (AFM) corroborated significant contraction of individual polymer chains due to intramolecular association of the BTA and UPy groups. The stepwise folding process resulting from orthogonal self-assembly-induced supramolecular interactions yields compartmentalized SCPNs comprised of distinct microdomains that mimick two secondary-structuring elements in proteins.”
“The geometric and subcellular organization of axon arbors distributes and regulates electrical signaling in neurons and networks, but the

underlying mechanisms have remained elusive. In rodent cerebellar cortex, stellate interneurons elaborate characteristic axon arbors that selectively innervate Purkinje cell dendrites and likely regulate dendritic integration. We used GFP BAC transgenic reporter mice to examine the cellular processes and molecular mechanisms underlying the development of stellate cell axons and their innervation pattern. We show that stellate axons are organized and guided towards Purkinje cell dendrites by an intermediate scaffold of Bergmann glial LY411575 purchase ( BG) fibers. The L1 family immunoglobulin protein Close Homologue of L1 ( CHL1) is localized to apical BG fibers and stellate cells during the development of stellate axon arbors. In the absence of CHL1, stellate axons deviate from BG fibers and show aberrant branching and orientation. Furthermore, synapse formation between aberrant stellate axons and Purkinje dendrites is reduced and cannot be maintained, leading to progressive atrophy of axon terminals. These results establish BG fibers as a guiding scaffold and CHL1 a molecular signal in the organization of stellate axon arbors and in directing their dendritic innervation.