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Hypothesis: Chemically or physically distinct patches can be induced on the micelles of amphiphilic block copolymers, which facilitate directional binding for the creation of hierarchical structures. Hence, control over the direction of patches on the micelles is a crucial factor to attain the directionality on the interactions between the micelles, particularly for generating colloidal molecules mimicking the symmetry of molecular structures. We hypothesized that direction and combination of the patches could be controlled by physical confinement of the micelles., Experiments: We first confined spherical micelles of diblock copolymers in topographic templates fabricated from nanopatterns of block copolymers by adjusting the coating conditions. Then, patch formation was conducted on the confined micelles by exposing them with a core-favorable solvent. Microscopic techniques of SEM, TEM, and AFM were employed to investigate directions of patches and structures of combined micelles in the template., Findings: The orientation of the patches on the micelles was guided by the physical confinement of the micelles in linear trenches. In addition, by confining the micelles in a circular hole, we obtained a specific polygon arrangement of the micelles depending on the number of micelles in the hole, which enabled the formation of cyclic colloidal molecules consisting of micelles., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Inc. All rights reserved.)

Patchy micelles of diblock copolymers can be polymerized into a linear supracolloidal chain. We measure the persistence and contour lengths of supracolloidal chains coated on a solid substrate to evaluate their flexibility. Based on the analysis, the chain is semi-flexible, and the conformation is suitably explained by the worm-like chain model. In addition, utilizing a spin-coating technique with the semi-flexible nature of the chains, we produce a self-supporting film of supracolloidal chains having nanoscale pores essentially from colloidal constituents that tend to form dense packing if there is no prior organization of them into a semi-flexible chain., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2021 Elsevier Inc. All rights reserved.)

Sodium phenylbutyrate is used for treating urea cycle disorders, providing an alternative for ammonia excretion. Following conversion to its CoA ester, phenylbutyryl-CoA is postulated to undergo one round of β-oxidation to phenylacetyl-CoA, the active metabolite. Molecular modeling suggests that medium chain acyl-CoA dehydrogenase (MCAD; EC 1.3.99.3), a key enzyme in straight chain fatty acid β-oxidation, could utilize phenylbutyryl-CoA as substrate. Moreover, phenylpropionyl-CoA has been shown to be a substrate for MCAD and its intermediates accumulate in patients with MCAD deficiency. We have examined the involvement of MCAD and other acyl-CoA dehydrogenases (ACADs) in the metabolism of phenylbutyryl-CoA. Anaerobic titration of purified recombinant human MCAD with phenylbutyryl-CoA caused changes in the MCAD spectrum that are similar to those induced by octanoyl-CoA, its bona fide substrate, and unique to the development of the charge transfer ternary complex. The calculated apparent dissociation constant (K(D app)) for these substrates was 2.16 μM and 0.12 μM, respectively. The MCAD reductive and oxidative half reactions were monitored using the electron transfer flavoprotein (ETF) fluorescence reduction assay. The catalytic efficiency and the K(m) for phenylbutyryl-CoA were 0.2 mM 34(-1)·sec(-1) and 5.3 μM compared to 4.0 mM(-1)·sec(-1) and 2.8 μM for octanoyl-CoA. Extracts of wild type and MCAD-deficient lymphoblast cells were tested for the ability to reduce ETF using phenylbutyryl-CoA as substrate. While ETF reduction activity was detected in extracts of wild type cells, it was undetectable in extracts of cells deficient in MCAD. The results are consistent with MCAD playing a key role in phenylbutyrate metabolism., (Copyright © 2012 Elsevier Inc. All rights reserved.)