Preparation of surface modified protein nanoparticles by introduction of sulfhydryl groups

Weber, Carolin; Reiß, Stephan; Langer, Klaus

doi:10.1016/s0378-5173(00)00590-1

Cited by 80 publications

(46 citation statements)

References 24 publications

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“…Furthermore, additional parameters such as the composition and the pH value of the HSA solution prior to the desolvation procedure and the purification of the nanoparticles were optimized in order to achieve a colloidal system with well-defined physicochemical characteristics. Such a system is a prerequisite if surface modification procedures aiming at specific drug binding and targeting properties are to be applied (Langer et al, 2000;Weber et al, 2000a).…”

Section: Resultsmentioning

confidence: 99%

“…In addition, we have studied the cellular uptake of these nanoparticles by confocal microscope imaging and FACS analysis. Together with our previous work on the covalent surface modification of such nanoparticles (Langer et al, 2000;Weber et al, 2000a) the study is intended to establish a rational basis for the production and application of protein-based nanoparticles as drug carrier systems.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Langer¹,

Balthasar²,

Vogel³

et al. 2003

International Journal of Pharmaceutics

661

491

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Langer¹,

Balthasar²,

Vogel³

et al. 2003

International Journal of Pharmaceutics

661

491

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“…1 They are biocompatible, metabolizable and amenable to surface modifications and ligand attachments for targeted delivery. [2][3][4] Desolvation is one of the common methods reported for protein nanoparticle synthesis, owing to its reproducibility and ease of preparation. 5,6 The process of removing/replacing solvating water molecules, by a non-solvent, from the hydration shell of a macromolecule is called desolvation.…”

Section: Introductionmentioning

confidence: 99%

The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug release

Ahsan¹,

Rao²

2017

IJN

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The process of moving hydrophobic amino acids into the core of a protein by desolvation is important in protein folding. However, a rapid and forced desolvation can lead to precipitation of proteins. Desolvation of proteins under controlled conditions generates nanoparticles – homogeneous aggregates with a narrow size distribution. The protein nanoparticles, under physiological conditions, undergo surface erosion due to the action of proteases, releasing the entrapped drug/gene. The packing density of protein nanoparticles significantly influences the release kinetics. We have investigated the desolvation process of gelatin, exploring the role of pH and desolvating agent in nanoparticle synthesis. Our results show that the desolvation process, initiated by the addition of acetone, follows distinct pathways for gelatin incubated at different pH values and results in the generation of nanoparticles with varying matrix densities. The nanoparticles synthesized with varying matrix densities show variations in drug loading and protease-dependent extra- and intracellular drug release. These results will be useful in fine-tuning the synthesis of nanoparticles with desirable drug release profiles.

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“…Protein nanoparticles may be used as a matrix in which a wide variety of drugs can be physically entrapped (3)(4)(5). In contrast to other nanoparticulate systems, they offer the benefit of carrying functional groups such as amino and carboxylic groups that can be used for surface modification (6)(7)(8). However, it is known that they can be rapidly removed from the blood circulation by the action of the immune system.…”

Section: Introductionmentioning

confidence: 99%

Optimization of PEGylation Conditions for BSA Nanoparticles Using Response Surface Methodology

et al. 2010

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Abstract. Chemical coupling of polyethylene glycol (PEG) to proteins or particles (PEGylation), prolongs their circulation half-life by greater than 50-fold, reduces their immunogenicity, and also promotes their accumulation in tumors due to enhanced permeability and retention effect. Herein, phase separation method was used to prepare bovine serum albumin (BSA) nanoparticles. PEGylation of BSA nanoparticles was performed by SPA activated mPEG through their free amino groups. Effect of process variables on PEGylation efficiency of BSA nanoparticles was investigated and optimized through response surface methodology with the amount of free amino groups as response. Optimum conditions was found to be 32.5 g/l of PEG concentration, PEG-nanoparticle incubation time of 10 min, incubation temperature of 27°C, and pH of 7 for 5 mg of BSA nanoparticles in 1 mL phosphate buffer. Analysis of data showed that PEG concentration had the most noticeable effect on the amount of PEGylated amino groups, but pH had the least. Mean diameter and zeta potential of PEGylated nanoparticles under these conditions were 217 nm and −14 mV, respectively. In conclusion, PEGylated nanoparticles demonstrated reduction of the negative surface charge compared to the non modified particles with the zeta potential of −31.7 mV. Drug release from PEGylated nanoparticles was almost slower than non-PEGylated ones, probably due to existence of a PEG layer around PEGylated particles which makes an extra resistance in opposition to drug diffusion.

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Preparation of surface modified protein nanoparticles by introduction of sulfhydryl groups

Cited by 80 publications

References 24 publications

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

Optimization of the preparation process for human serum albumin (HSA) nanoparticles

The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug release

Optimization of PEGylation Conditions for BSA Nanoparticles Using Response Surface Methodology

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