Summary: Amphiphilic cylindrical brush‐coil block copolymers consisting of a polystyrene coil and a cylindrical brush block with poly(acrylic acid) side chains are prepared by ATRP of t‐butylacrylate from a block comacroinitiator. Upon acidolysis of the poly(t‐butylacrylate), water‐soluble polymers were obtained that were observed to form micelles consisting of 4–5 block copolymers on average in aqueous solution. The star‐like nature of such micelles was clearly visualized by scanning force microscopy.Schematic of coil‐cylindrical brush block copolymer PS‐b‐(PiBEMA‐g‐PAA), its AFM image clearly showing the main chain and the PAA corona of the cylindrical brush block.magnified imageSchematic of coil‐cylindrical brush block copolymer PS‐b‐(PiBEMA‐g‐PAA), its AFM image clearly showing the main chain and the PAA corona of the cylindrical brush block.

Self-assembled helices were used as templates to form helical mesopores in a polymeric matrix. The template was formed from the self-association of 3,5-bis(5-hexylcarbamoylpentyloxy)benzoic acid decyl ester in ethylene glycol diacrylate. The monomer was photopolymerized, and the resulting resin was extracted to remove the template. The helical shape of the pores was proven by TEM and tomographic studies. The ability to form material with high specific areas using tubular templates from the same molecules was also shown.

Summary: We report the synthesis of a new enzymatically degradable gel based on PHEMA and PEO crosslinking macromonomer. The crosslinker contains the tripeptide sequence Gly‐Gly‐Leu, which is a substrate for proteases such as subtilisin or chymotrypsin. The crosslinker was obtained by the coupling reaction of succinyl‐glycyl‐glycyl‐leucine with 2‐aminoethyl‐terminated PEO chains ($\overline M _{\rm w}$ = 3 400) and subsequent esterification of the hydroxyl endgroup with methacryloyl chloride. It was characterized by SEC and 1H NMR. Enzymatic cleavage of the crosslinking macromonomer was showed by SEC. The macromonomer was copolymerized with HEMA to yield hydrogel that is stable in a physiological buffer. Enzymatic assay showed that this gel is degraded in the presence of a bacterial protease (subtilisin). The degradation is complete within 50 d at 37 °C. This new gel is a good candidate for drug‐delivery systems where the release can be triggered by the presence of bacterial proteases.

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