25 research outputs found
Well-defined protein-polymer conjugatesâsynthesis and potential applications
During the last decades, numerous studies have focused on combining the unique catalytic/functional properties and structural characteristics of proteins and enzymes with those of synthetic molecules and macromolecules. The aim of such multidisciplinary studies is to improve the properties of the natural component, combine them with those of the synthetic, and create novel biomaterials in the nanometer scale. The specific coupling of polymers onto the protein structures has proved to be one of the most straightforward and applicable approaches in that sense. In this article, we focus on the synthetic pathways that have or can be utilized to specifically couple proteins to polymers. The different categories of well-defined protein-polymer conjugates and the effect of the polymer on the protein function are discussed. Studies have shown that the specific conjugation of a synthetic polymer to a protein conveys its physico-chemical properties and, therefore, modifies the biodistribution and solubility of the protein, making it in certain cases soluble and active in organic solvents. An overview of the applications derived from such bioconjugates in the pharmaceutical industry, biocatalysis, and supramolecular nanobiotechnology is presented at the final part of the articl
Copper mediated polymerization without external deoxygenation or oxygen scavengers
Overcoming the challenge of rigorous deoxygenation in copper mediated controlled radical polymerization processes (e.g. ATRP), we report a simple Cu(0)âRDRP system in the absence of external additives (e.g. reducing agents, enzymes etc.). By simply adjusting the headspace of the reaction vessel, a wide range of monomers, namely acrylates, methacrylates, acrylamides and styrene, can be polymerized in a controlled manner yielding polymers with low dispersities, nearâquantitative conversions and high end group fidelity. Significantly, this approach is scalable (~ 125 g), tolerant to elevated temperatures, compatible with both organic and aqueous media and does not rely on external stimuli which may limit the monomer pool. The robustness and versatility of this methodology is further demonstrated by the applicability to a number of other copper mediated techniques including conventional ATRP and lightâmediated approaches
Correctly validating results from single molecule data: the case of stretched exponential decay in the catalytic activity of single lipase B molecules
The question of how to validate and interpret correctly the waiting time
probability density functions (WT-PDFs) from single molecule data is addressed.
It is shown by simulation that when a stretched exponential WT-PDF, with a
stretched exponent alfa and a time scale parameter tau, generates the off
periods of a two-state trajectory, a reliable recovery of the input WT-PDF from
the trajectory is obtained even when the bin size used to define the
trajectory, dt, is much larger than the parameter tau. This holds true as long
as the first moment of the WT-PDF is much larger than dt. Our results validate
the results in an earlier study of the activity of single Lipase B molecules
and disprove recent related critique
Nanosized carriers based on amphiphilic poly-N-vinyl-2-pyrrolidone for intranuclear drug delivery
In situ ATRP-mediated hierarchical formation of giant amphiphile bionanoreactors
Amphiphilic bioconjugates can be synthesized in situ by grafting polystyrene from a protein. The resulting giant amphiphiles display low polydispersities and the characteristic aggregation properties of amphiphilic biomacromolecules. A second, catalytically active guest protein can also be included within the superstructures
Well-defined protein-polymer conjugates-synthesis and potential applications
During the last decades, numerous studies have focused on combining the unique catalytic/functional properties and structural characteristics of proteins and enzymes with those of synthetic molecules and macromolecules. The aim of such multidisciplinary studies is to improve the properties of the natural component, combine them with those of the synthetic, and create novel biomaterials in the nanometer scale. The specific coupling of polymers onto the protein structures has proved to be one of the most straightforward and applicable approaches in that sense. In this article, we focus on the synthetic pathways that have or can be utilized to specifically couple proteins to polymers. The different categories of well-defined protein-polymer conjugates and the effect of the polymer on the protein function are discussed. Studies have shown that the specific conjugation of a synthetic polymer to a protein conveys its physico-chemical properties and, therefore, modifies the biodistribution and solubility of the protein, making it in certain cases soluble and active in organic solvents. An overview of the applications derived from such bioconjugates in the pharmaceutical industry, biocatalysis, and supramolecular nanobiotechnology is presented at the final part of the article
Formation of giant amphiphiles by post-functionalization of hydrophilic protein-polymer conjugates
A novel, generic method for the synthesis of families of tri-block protein-polymer giant amphiphiles was designed and developed. We have synthesized a hydrophilic alpha-maleimido poly-1-alkyne with M-n = 9.5 kDa (H-1-NMR) and narrow PDi (1.15 as measured by SEC) via ATRP (Atom Transfer Radical Polymerization). This polymer was successfully coupled to BSA to afford a hydrophilic multifunctional bioconjugate which was isolated using protein purification techniques and fully characterized. Following the post-functionalization approach, we introduced hydrophobicity to the resulting hydrophilic biohybrid by a straightforward, high yield "click'"-chemistry cycloaddition step. The resulting tri-block protein-polymer amphiphiles were isolated and showed interesting aggregation patterns (TEM, confocal microscopy)
Modulation of Entrapment Efficiency and In Vitro Release Properties of BSA-Loaded Chitosan Microparticles Cross-Linked with Citric Acid as a Potential ProteinâDrug Delivery System
Microparticles, aimed for oral protein and peptide drug delivery, were prepared via emulsion cross-linking using citric acid as cross-linker and polyglycerol polyricinoleate as surfactant. A comparative study of the interaction between chitosan and citric acid and its effect on the resulting microparticle properties was performed using different chitosan-to-cross-linker mass ratios and pH-values during fabrication of the microparticles. Non-cross-linked and cross-linked microparticles were studied in terms of size (4–12 μm), zeta potential (−15.7 to 12.8 mV), erosion (39.7–75.6%), a model protein encapsulation efficiency (bovine serum albumin) (6.8–27.6%), and loading capacity (10.4–40%). Fourier transform infrared spectroscopy and X-ray diffraction confirmed the ionic interaction between the protonated amine groups of chitosan and the carboxylate ions of the cross-linking agent. Scanning electron microscopy revealed that the non-cross-linked microparticles had an uneven shape with wrinkled surfaces, while the cross-linked formulations were spherical in shape with smooth surfaces. On the basis of these data, the role of the surfactant and microparticle structure on the release mechanism was proposed. Control of the microparticle shape and release mechanisms is expected to be crucial in developing carriers for the controlled delivery of proteins and peptides