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Related Concept Videos

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Surface Passivation for Single-molecule Protein Studies
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Process for protein PEGylation.

David Pfister1, Massimo Morbidelli1

  • 1Institute for Chemical and Bioengineering, ETH, Wolfgang-Pauli-Str. 10, 8093 Zurich, Switzerland.

Journal of Controlled Release : Official Journal of the Controlled Release Society
|February 18, 2014
PubMed
Summary
This summary is machine-generated.

PEGylation enhances drug delivery by increasing protein persistence in the body. Optimizing PEGylation reaction engineering and purification is key for cost-effective, industrial-scale therapeutic protein production.

Keywords:
BioengineeringDrug deliveryPEGylationReaction engineeringSeparation

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Area of Science:

  • Bioconjugation Chemistry
  • Drug Delivery Systems
  • Process Engineering

Background:

  • PEGylation is a crucial technique in drug delivery, offering diverse conjugation chemistry and polymer structures.
  • It enhances therapeutic protein persistence in vivo without compromising activity.
  • High production costs of therapeutic proteins necessitate optimization of PEGylation processes.

Purpose of the Study:

  • To critically review the state-of-the-art in PEGylation reaction engineering and purification.
  • To focus on developing industrial-scale processes meeting market quality and cost requirements.
  • To explore the integration of continuous reaction and separation steps.

Main Methods:

  • Review of current literature on PEGylation reaction engineering.
  • Analysis of purification strategies for PEGylated proteins.
  • Evaluation of continuous processing and integrated reaction-separation systems.

Main Results:

  • Identified key challenges and advancements in PEGylation reaction engineering for industrial scale.
  • Highlighted optimized purification techniques to reduce costs and maintain protein activity.
  • Demonstrated the potential of integrated continuous processes for efficient manufacturing.

Conclusions:

  • Optimized PEGylation reaction engineering and purification are essential for cost-effective therapeutic protein production.
  • Continuous processing offers a promising avenue for scalable and efficient PEGylation.
  • Further development in these areas will facilitate market access for advanced biologic drugs.