Preparation and characterization of protein-loaded N-trimethyl chitosan nanoparticles as nasal delivery system

Amidi, Maryam; Romeijn, Stefan; Borchard, Gerrit; Junginger, Hans E.; Hennink, Wim E.; Jiskoot, Wim

doi:10.1016/j.jconrel.2005.11.014

Cited by 366 publications

(163 citation statements)

References 55 publications

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“…However, at that time a steady state is achieved and no further release is observed up to 24h. This initial burst release might correspond to the amount of protein that is located at the surface of the nanoparticles, which thus easily desorbs, an effect that has been reported in other studies (Amidi et al, 2006). Other works available in the literature describe quite similar release behaviour.…”

Section: Preparation and Characterisation Of Nanoparticlessupporting

confidence: 68%

“…Figure 3 shows the in vitro release of BSA in PBS pH 7.4, a medium that intends to resemble the environment of mucosal surfaces like the pulmonary (Walters, 2002), although in some cases it has also been used in the context of nasal delivery (Amidi et al, 2006;Amidi et al, 2007;Fernández-Urrusuno et al, 1999a). Results indicate that, for both formulations, the release of BSA from nanoparticles shows an initial burst, releasing approximately 30% of the encapsulated protein in 2h.…”

Section: Preparation and Characterisation Of Nanoparticlesmentioning

confidence: 99%

“…Other works available in the literature describe quite similar release behaviour. N-trimethylchitosan nanoparticles designed for nasal delivery also released rapidly (3h) 30% of the associated protein in the same medium, although the assay was not prolonged beyond that (Amidi et al, 2006). In chitosan/ tripolyphosphate nanoparticles it has been seen that BSA releases very slowly, for several days (Calvo et al, 1997a, b;Gan and Wang, 2007).…”

Section: Preparation and Characterisation Of Nanoparticlesmentioning

confidence: 99%

See 2 more Smart Citations

Pullulan-based nanoparticles as carriers for transmucosal protein delivery

Dionísio

Cordeiro

Remuñán‐López

et al. 2013

European Journal of Pharmaceutical Sciences

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Polymeric nanoparticles have revealed very effective in transmucosal delivery of proteins. Polysaccharides are among the most used materials for the production of these carriers, owing to their structural flexibility and propensity to evidence biocompatibility and biodegradability. In parallel, there is a preference for the use of mild methods for their production, in order to prevent protein degradation, ensure lower costs and easier procedures that enable scaling up.In this work we propose the production of pullulan-based nanoparticles by a mild method of polyelectrolyte complexation. As pullulan is a neutral polysaccharide, sulfated and aminated derivatives of the polymer were synthesized to provide pullulan with a charge. These derivatives were then complexed with chitosan and carrageenan, respectively, to produce the nanocarriers. Positively charged nanoparticles of 180-270 nm were obtained, evidencing ability to associate bovine serum albumin, which was selected as model protein. In PBS pH 7.4, pullulan-based nanoparticles were found to have a burst release of 30% of the protein, which maintained up to 24h. Nanoparticle size and zeta potential were preserved upon freeze-drying in the presence of appropriate cryoprotectants. A factorial design was approached to assess the cytotoxicity of raw materials and nanoparticles by the metabolic test MTT. Nanoparticles demonstrated to not cause overt toxicity in a respiratory cell model (Calu-3). Pullulan has, thus, demonstrated to hold potential for the production of nanoparticles with an application in protein delivery.

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Section: Preparation and Characterisation Of Nanoparticlessupporting

confidence: 68%

Section: Preparation and Characterisation Of Nanoparticlesmentioning

confidence: 99%

Section: Preparation and Characterisation Of Nanoparticlesmentioning

confidence: 99%

See 1 more Smart Citation

Pullulan-based nanoparticles as carriers for transmucosal protein delivery

Dionísio

Cordeiro

Remuñán‐López

et al. 2013

European Journal of Pharmaceutical Sciences

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“…Besides, hemolysis of the PECs suspensions was always lower than 1% when tested against mouse RBC (Figure 3), clearly below the 5% value considered as the toxicity threshold. These results are in agreement with other reports on TMC based nanovectors with low toxicity 46 and also show a correlation of the cytotoxicity with other structural parameters besides surface charge, like size of the 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 nanoparticles, molecular weight of chitosan and acetylation degree. 47 Moreover, the lowered buffering capacity of chitosan after methylation 5 prevents endo-lysosomal disruption and scape, 48 which in combination with the dissociation capacity of the PECs at low pH 5 and the eventual TMC degradation by lysosomal enzymes, 49 may preserve lysosomal function after PECs internalization.…”

Section: Specific Enzymatic Activity and Activity In Primary Culturessupporting

confidence: 94%

Highly Versatile Polyelectrolyte Complexes for Improving the Enzyme Replacement Therapy of Lysosomal Storage Disorders

Giannotti

Abasolo

Oliva

et al. 2016

ACS Appl. Mater. Interfaces

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“…Generally, size distributions with polydispersity indices of less than 0.1 are considered to be monodisperse. 36,37 Effect of ion identity, ionic strength, and pH on the self-association of peptibody A The PbA s w values (and hence self-association) were observed to be very sensitive to ionic strength as well as anion identity. For a fixed PbA concentration (1 mg/mL) and a given NaX (X ¼ halogen ion) concentration, the s w values increased with the atomic size of the monovalent anion [ Fig.…”

Section: Solution Behavior Of Peptibody Amentioning

confidence: 99%

Ion‐specific modulation of protein interactions: Anion‐induced, reversible oligomerization of a fusion protein

et al. 2008

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Ions can significantly modulate the solution interactions of proteins. We aim to demonstrate that the salt-dependent reversible heptamerization of a fusion protein called peptibody A or PbA is governed by anion-specific interactions with key arginyl and lysyl residues on its peptide arms. Peptibody A, an E. coli expressed, basic (pI 5 8.8), homodimer (65.2 kDa), consisted of an IgG1-Fc with two, C-terminal peptide arms linked via penta-glycine linkers. Each peptide arm was composed of two, tandem, active sequences (SEYQGL PPQGWK) separated by a spacer (GSGSATGGSGGGASSGSGSATG). PbA was monomeric in 10 mM acetate, pH 5.0 but exhibited reversible self-association upon salt addition. The sedimentation coefficient (s w ) and hydrodynamic diameter (D H ) versus PbA concentration isotherms in the presence of 140 mM NaCl (A5N) displayed sharp increases in s w and D H , reaching plateau values of 9 s and 16 nm by 10 mg/mL PbA. The D H and sedimentation equilibrium data in the plateau region (>12 mg/mL) indicated the oligomeric ensemble to be monodisperse (PdI 5 0.05) with a z-average molecular weight (M z ) of 433 kDa (stoichiometry 5 7). There was no evidence of reversible selfassociation for an IgG1-Fc molecule in A5N by itself or in a mixture containing fluorescently labeled IgG1-Fc and PbA, indicative of PbA self-assembly being mediated through its peptide arms. Self-association increased with pH, NaCl concentration, and anion size (I 2 > Br 2 > Cl 2 > F 2 ) but could be inhibited using soluble Trp-, Phe-, and Leu-amide salts (Trp > Phe > Leu). We propose that in the presence of salt (i) anion binding renders PbA self-association competent by neutralizing the peptidyl arginyl and lysyl amines, (ii) self-association occurs via aromatic and hydrophobic interactions between the ..xx ..xxx.. xx.. motifs, and (iii) at >10 mg/mL, PbA predominantly exists as heptameric clusters.Keywords: Hofmeister series; electroselectivity series; self-association; ion-protein interactions; anion binding; dynamic light scattering; analytical ultracentrifugation Abbreviations: A5, 10 mM acetate buffer at pH 5.0; A5N, 10 mM acetate buffer at pH 5.0 containing 140 mM sodium chloride;

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Preparation and characterization of protein-loaded N-trimethyl chitosan nanoparticles as nasal delivery system

Cited by 366 publications

References 55 publications

Pullulan-based nanoparticles as carriers for transmucosal protein delivery

Pullulan-based nanoparticles as carriers for transmucosal protein delivery

Highly Versatile Polyelectrolyte Complexes for Improving the Enzyme Replacement Therapy of Lysosomal Storage Disorders

Ion‐specific modulation of protein interactions: Anion‐induced, reversible oligomerization of a fusion protein

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