Controlling and Switching the Morphology of Micellar Nanoparticles with Enzymes

Abstract

Micelles were prepared from polymer-peptide block copolymer amphiphiles containing substrates for protein kinase A, protein phosphatase-1 and matrix metalloproteinases 2 and 9. We examine reversible switching of the morphology of these micelles through a phosphorylation-dephosphorylation cycle and study peptide-sequence directed changes in morphology in response to proteolysis. Furthermore, the exceptional uniformity of these polymer-peptide particles makes them amenable to cryo-TEM reconstruction techniques lending insight into their internal structure.

Understanding the catalytic activity of single‐chain polymeric nanoparticles in water

“…On the other hand, creating sufficiently hydrophobic domains around the catalytic sites to ensure compatibility of the homogeneous organo-or metal-based catalysts with aqueous environments has remained a major challenge. [1][2][3] For this reason, artificial metalloenzymes, [4][5][6] DNA-based catalysts, 7 amphiphilic copolymers, [8][9][10] star polymers, [11][12][13][14][15] micellar systems, [16][17][18][19][20] molecularly imprinted nano and microgels, [21][22][23] and dendrimers [24][25][26][27][28] were designed to achieve the necessary compartmentalization for efficient catalysis in water. Supramolecular folding of polymer chains into single chain polymeric nanoparticles (SCPNs) is an attractive alternative to prepare compartmentalized, water-soluble, nanometersized particles with a hydrophobic interior.…”

Magnetic surfactants

“…A more sophisticated approach is to use external stimuli to activate reversible changes in molecular structures with responsive surfactants [5]. This has been achieved through sensitivity towards changes in CO2 levels [6], light [7], enzymes [8] and electrical potential (redox) [9]. Interestingly, many of the redox-active surfactants would also be expected to be paramagnetic.…”

Enzymatically Triggered, Isothermally Responsive Polymers: Reprogramming Poly(oligoethylene glycols) To Respond to Phosphatase

“…12 They can also provide valuable biomarkers with a range of stress and disease states characterised by imbalances in enzyme expression and activity. 13 For instance, hepsin is a protease overexpressed in the early stages of prostate cancer, 14 cathepsins are released at inflammatory sites 15 and widely used as a release mechanism in polymer-drug conjugates and matrix metalloproteinases have been linked to vascular disease and tumour growth. 16,17 The use of enzymes to trigger a specific response and hence manipulate the structures and pharmacokinetics of polymer-based materials has received increasing attention.…”