Stabilizing and destabilizing protein surfactant-based foams in the presence of a chemical surfactant: Effect of adsorption kinetics

Li, Huazhen; Agyei, Dominic; Shen, Wei; Middelberg, Anton P. J.; He, Lizhong

doi:10.1016/j.jcis.2015.08.068

Cited by 9 publications

(2 citation statements)

References 31 publications

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“…As DAMP4 consists of four AM1 units it is not possible to distinguish between them by XRR. This modelled density profile showed that for DAMP4, there is a surface excess layer about 11 Å thick with a higher electron density than pure water, as has been previously observed (Dwyer et al, 2013, Li et al, 2016. For a solution containing 5K-PEG-Hi PEGylated DAMP4 there is a surface layer with a slight reduced electron density suggesting that the surface packing of the DAMP4 may be disrupted.…”

Section: Interfacial Thickness Of the Peg Layersupporting

confidence: 72%

Refining nanocarrier emulsions for pharmaceutical use

Tayeb¹

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Nanomaterials with different surface designs and biophysical properties are being developed to improve the efficacy of hydrophobic drugs. To date, these improvements have not overcome the complexity of biological and physical barriers via different delivery routes, however, nanoemulsions (NEs), in particular tailorable nanocarrier emulsions (TNEs), are emerging as promising drug carriers. The novel oil-in-water NEs are stabilised with chemically-engineered biosurfactants (AM1) that allow top-down sequential addition and modification with a chemically-related 4-helix bundle protein, DAMP4, which can be fused to various biomolecules. In this project, the feasibility of using TNEs for diagnostic/therapeutic applications via different delivery routes was investigated. The initially stages of the work were to evaluate the encapsulation and retention capacity of hydrophobic compounds within the oil core of TNEs with varying surface properties. Polyethylene glycol (PEG), an important pharmaceutical tool, was chemically conjugated to DAMP4 and influenced cargo retention within the oil core. In collaboration with Professor Tarl Prow, tuning the TNE surface charge, which was found to be indirectly related to PEG density, allowed TNEs to coat elongated microparticles via electrostatic interactions, creating a promising tool for topical drug delivery. Cofunctionalising TNEs with antibody fragments showed receptor-specific targeting in vitro, however, in vivo active targeting was not achieved following intravenous administration. Biodistribution

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Section: Interfacial Thickness Of the Peg Layersupporting

confidence: 72%

Refining nanocarrier emulsions for pharmaceutical use

Tayeb¹

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“…reported elsewhere (Li et al 2016) with slight modification in lysis buffer (50 mM Na2HPO4, 500 mM NaCl), equilibrium buffer (lysis buffer + 20 mM imidazole), and elution buffer (lysis buffer + 500 mM imidazole).…”

Section: Affinity Chromatography Purificationmentioning

confidence: 99%

Murine polyomavirus VLPs as a platform for cytotoxic T cell epitope-based influenza vaccine candidates

Abidin¹

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This research examined the ability of virus-like particles (VLP) assembled from the coat proteins of Murine polyomavirus (MPyV) to carry cytotoxic T cell (Tc) epitopes. MPyV VLPs can be assembled in vitro from purified subunits composed of pentamers of the major coat protein VP1 called capsomeres; and this approach provides fine control over VLP composition and structure. Tc-epitopes are often highly hydrophobic, which poses a significant bioengineering challenge and two distinct approaches were pursued to determine the optimal delivery strategy of Influenza Tc-epitopes by MPyV VLP. Firstly, identified epitopes were externally presented using established sites for peptide insertion on the MPyV major coat protein, VP1. Secondly, polypeptides possessing multiple epitopes were encapsidated within VP1 VLP using precise elements of the minor coat protein VP2/3 that interact with the interior cavity of capsomeres. Hydrophobicity-related capsomere aggregation arising from single Tc epitope presentation was successfully circumvented by engineering charged amino acids (DD) flanking the epitope displayed on a surface-exposed loop of VP1 and by use of an optimised buffer condition. A multiparametric, high-throughput buffer screen was implemented to optimise pH and buffer additives during affinity tag removal. Stable modified capsomere recovered from this reaction were assembly competent in the presence of L-Arginine, and VLP yield was high when modular capsomeres were co-assembled with unmodified VP1 capsomeres forming stable mosaic VLPs. The ability of the MPyV VLP to encapsidate foreign protein was first evaluated and optimised with green fluorescent protein (GFP) as a model protein to enable monitoring and analysis.A minimal VP1-interacting sequence was defined from the carboxy-terminus of VP2/3 (VP2C) and fused to the amino-terminus of GFP, ensuring internalisation of the reporter protein. VP1:VP2C-GFP capsomere complexes were successfully recovered when VP1 was co-expressed with VP2C-GFP, whereas complex formation was not observed when VP1 and VP2C-GFP were mixed in vitro.Recovered capsomere complexes were assembly competent and amount of encapsidated GFP was controllable when VP1:VP2C-GFP capsomere complexes were co-assembled with unmodified VP1 capsomeres in a defined molar ratio. The encapsidation approach was then applied to a subdomain of the Influenza matrix protein M1 by co-expressing VP1 with VP2C-M1-I. M1-I capsomere complexes were assembly competent as indicated by gel electrophoresis, dynamic light scattering, and transmission electron microscopy. To enable recovery of VLPs for analysis and characterisation as well as to confirm encapsidation and the formation of mosaic VLPs, a semi-preparative size exclusion chromatography method was developed. This research was able to address bioengineering challenges posed by hydrophobic epitope presentation and developed MPyV

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Design of Stimuli‐Responsive Peptides and Proteins

Yang

Gerstweiler

et al. 2022

Adv Funct Materials

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Stimuli‐responsive peptides and proteins are an exciting class of smart biomaterials for various applications and have received significant attention over the past decades. A wide variety of stimuli such as temperature, pH, ions, enzymes, magnetic field, redox, etc., are explored. This article provides a review of five intensively studied types of stimuli‐responsive peptides and proteins, their design principles and applications, including temperature‐, pH‐, light‐, metal ion‐, and enzyme‐responsive with an emphasis on the key design concepts and switch function. Moreover, typical examples of their applications are discussed to provide a better understanding of the design concept and underlying methodology. This review will facilitate and inspire future innovation toward new peptide‐ and protein‐based materials and their diverse applications.

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Stabilizing and destabilizing protein surfactant-based foams in the presence of a chemical surfactant: Effect of adsorption kinetics

Cited by 9 publications

References 31 publications

Refining nanocarrier emulsions for pharmaceutical use

Refining nanocarrier emulsions for pharmaceutical use

Murine polyomavirus VLPs as a platform for cytotoxic T cell epitope-based influenza vaccine candidates

Design of Stimuli‐Responsive Peptides and Proteins

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