Polymerization Induced Self-Assembly of a Site-Specific Interferon α-Block Copolymer Conjugate into Micelles with Remarkably Enhanced Pharmacology

A hierarchically structured platform was obtained from spontaneous self-assembly of a poly(styrene)-<i>b</i>-poly(vinylbenzylchloride) (PS-<i>b</i>-PVBC) block copolymer (BCP) during breath figure (BF) templating. The BF process using a water/ethanol atmosphere gave a unique double porosity in which hexagonally arranged micron-sized pores were encircled by a secondary population of smaller, nano-sized pores. A third level of structuration was simultaneously introduced between the pores by directed BCP self-assembly to form out-of-the-plane nano-cylinders, offering very rapid bottom-up access to a film with unprecedented triple structure which could be used as a reactive platform for introducing further surface functionality. The surface nano-domains of VBC were exploited as reactive nano-patterns for site-specific chemical functionalization by firstly substituting the exposed chlorine moiety with azide, then “clicking” an alkyne by copper (I) catalyzed azide-alkyne Huisgen cycloaddition (CuAAC). Successful chemical modification was verified by NMR spectroscopy, FTIR spectroscopy, and XPS, with retention of the micro- and nanostructuration confirmed by SEM and AFM respectively. Protonation of the cyclotriazole surface groups triggered a switch in macroscopic behavior from a Cassie-Baxter state to a Wenzel state, highlighting the possibility of producing responsive surfaces with hierarchical structure.

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The Self-Assembly of an Amphiphilic Block Copolymer: A Dissipative Particle Dynamics Study

Tenside Surfactants Detergents ◽

10.3139/113.100254 ◽

2005 ◽

Vol 42 (3) ◽

pp. 180-183 ◽

Cited By ~ 2

Author(s):

S. G. Schulz ◽

U. Frieske ◽

H. Kuhn ◽

G. Schmid ◽

F. Müller ◽

...

Keyword(s):

Block Copolymer ◽

Self Assembly ◽

Dissipative Particle Dynamics ◽

Particle Dynamics ◽

The Self ◽

Amphiphilic Block Copolymer

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Faculty Opinions recommendation of A mutation in the Mod subunit of EcoP15I restriction enzyme converts the DNA methyltransferase to a site-specific endonuclease.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1074805.527727 ◽

2007 ◽

Author(s):

Narayanaswamy Srinivasan

Keyword(s):

Restriction Enzyme ◽

Dna Methyltransferase ◽

Site Specific ◽

A Site

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Faculty Opinions recommendation of A site-specific, multiplexed kinase activity assay using stable-isotope dilution and high-resolution mass spectrometry.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1161908.623533 ◽

2009 ◽

Author(s):

Jonathan Chernoff

Keyword(s):

Mass Spectrometry ◽

High Resolution ◽

Kinase Activity ◽

High Resolution Mass Spectrometry ◽

Activity Assay ◽

Site Specific ◽

Stable Isotope Dilution ◽

A Site ◽

Kinase Activity Assay ◽

Resolution Mass

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DECADAL SUMMER LAKE WATER TEMPERATURE VARIABILITY IN SOUTHERN GREENLAND OF THE LAST 2 MILLENNIA: DEVELOPMENT AND APPLICATION OF A SITE-SPECIFIC BRGDGT CALIBRATION

10.1130/abs/2020am-355583 ◽

2020 ◽

Author(s):

Boyang Zhao ◽

◽

Isla S. Castañeda ◽

Raymond S. Bradley ◽

Jeff Salacup ◽

...

Keyword(s):

Water Temperature ◽

Lake Water ◽

Temperature Variability ◽

Site Specific ◽

A Site

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Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene.

Molecular and Cellular Biology ◽

10.1128/mcb.9.4.1507 ◽

1989 ◽

Vol 9 (4) ◽

pp. 1507-1512 ◽

Cited By ~ 22

Author(s):

H Zhu ◽

H Conrad-Webb ◽

X S Liao ◽

P S Perlman ◽

R A Butow

Keyword(s):

Genetic Analysis ◽

Rna Processing ◽

Fold Increase ◽

Functional Expression ◽

Rrna Gene ◽

Yeast Mitochondria ◽

Wild Type ◽

Site Specific ◽

Var1 Gene ◽

A Site

All mRNAs of yeast mitochondria are processed at their 3' ends within a conserved dodecamer sequence, 5'-AAUAAUAUUCUU-3'. A dominant nuclear suppressor, SUV3-I, was previously isolated because it suppresses a dodecamer deletion at the 3' end of the var1 gene. We have tested the effects of SUV3-1 on a mutant containing two adjacent transversions within a dodecamer at the 3' end of fit1, a gene located within the 1,143-base-pair intron of the 21S rRNA gene, whose product is a site-specific endonuclease required in crosses for the quantitative transmission of that intron to 21S alleles that lack it. The fit1 dodecamer mutations blocked both intron transmission and dodecamer cleavage, neither of which was suppressed by SUV3-1 when present in heterozygous or homozygous configurations. Unexpectedly, we found that SUV3-1 completely blocked cleavage of the wild-type fit1 dodecamer and, in SUV3-1 homozygous crosses, intron conversion. In addition, SUV3-1 resulted in at least a 40-fold increase in the amount of excised intron accumulated. Genetic analysis showed that these phenotypes resulted from the same mutation. We conclude that cleavage of a wild-type dodecamer sequence at the 3' end of the fit1 gene is essential for fit1 expression.

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