Encapsulation-induced aggregation and loss in activity of γ-chymotrypsin and their prevention

Castellanos, Ingrid J.; Cruz, Gloydian; Crespo, Rubén; Griebenow, Kai

doi:10.1016/s0168-3659(02)00073-1

Cited by 70 publications

(65 citation statements)

References 42 publications

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“…In our study, both cases exhibited high recovery rates. These results indicate that PLGA did not nearly affect recovery rates of 3D8 scFv, not consistent with other previous results (Castellanos et al, 2002;van de Weert et al, 2000a,b). This is probably attributed to the nature of 3D8 scFv.…”

Section: Discussionsupporting

confidence: 73%

“…aggregates or cause aggregate formation. Also, irreversible conformational changes of proteins may occurred by the extraction media (Castellanos et al, 2002). The efficiency of protein recovery is generally low (Kang et al, 2002;van de Weert et al, 2000a,b;Johansen et al, 1998;Sharif and O'Hagan, 1995;Sah, 1997) because PLGA tends to precipitate out with encapsulated protein due to the addition of excess buffer (van de Weert et al, 2000a,b).…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, in case of the recovery of 3D8 scFv was comparatively high as compared with other proteins or Abs. Furthermore, several studies have shown that the degree of recovery from protein aqueous solution indicates the extent of protein adsorption at the W/O interface (Castellanos et al, 2002;van de Weert et al, 2000a,b;Johansen et al, 1998). But, significant changes in the recovery rates of 3D8 scFv were not observed depending on stabilizer species including sugars, polyols and hydrophilic polymer.…”

Section: Discussionmentioning

confidence: 99%

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Optimized stability retention of a monoclonal antibody in the PLGA nanoparticles

Son

Lee

Joung

et al. 2009

International Journal of Pharmaceutics

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Optimized stability retention of a monoclonal antibody in the PLGA nanoparticles

Son

Lee

Joung

et al. 2009

International Journal of Pharmaceutics

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“…Furthermore, Castellanos et al (2002) address the effects of various physical and chemical parameters on the integrity and activity of encapsulated -chymotrypsin.…”

Section: Release Of -Chymotrypsin From Optimised Particlesmentioning

confidence: 99%

Encapsulation and release ofα-chymotrypsin from poly(glycerol adipate-co-ω-pentadecalactone) microparticles

Gaskell¹,

Hobbs²,

Rostron³

et al. 2008

Journal of Microencapsulation

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Polymer based microparticles are increasingly becoming of interest for a variety of applications including drug delivery. Recently poly(glycerol adipate) (PGA) and poly(glycol adipate-co--pentadecalactone) have shown promise for delivery of dexamethasone phosphate and ibuprofen. In this paper the copolyester poly(glycol adipate-co--pentadecalactone) was evaluated as a colloidal delivery system for encapsulated therapeutic proteins. Enzyme containing microparticles were prepared via the double water-in-oil-in-water (w/o/w) emulsion-solvent evaporation methodology. -chymotrypsin was used as a model proteolytic enzyme and its transfer was monitored during the emulsification process, in addition to in vitro release from formed particles. On average 22.1g protein per 1mg polymer was encapsulated, although gradual loss of activity of the protein, once released, was recorded. The work presented shows the potential of this polyester as a delivery system for enzymes via microparticles, with improvements to the system achievable via polymer and process optimisation. The pendant hydroxyl groups on the polymer backbone provide future capacity for tailored alteration of the physical and chemical properties of the polymer, in addition to covalent attachment of various compounds.

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“…Difficulties in the encapsulation of proteins are related to their high molecular weight (M W) , high water solubility and instability upon exposure to formulation conditions 5 . An initial burst release followed by slow, incomplete release of the native protein as a result of protein instability and aggregation has also been recognized as a major problem 6 . Interactions between the protein and the polymer also influence the release profile.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of biodegradable polyester-co-lactone microparticles for protein delivery

Tawfeek

Khidr

Samy

et al. 2013

Drug Development and Industrial Pharmacy

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Encapsulation-induced aggregation and loss in activity of γ-chymotrypsin and their prevention

Cited by 70 publications

References 42 publications

Optimized stability retention of a monoclonal antibody in the PLGA nanoparticles

Optimized stability retention of a monoclonal antibody in the PLGA nanoparticles

Encapsulation and release ofα-chymotrypsin from poly(glycerol adipate-co-ω-pentadecalactone) microparticles

Evaluation of biodegradable polyester-co-lactone microparticles for protein delivery

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