Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Folding01:25

Protein Folding

12.6K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

711
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
711

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Predictors and Economic Impact of Red Blood Cell Transfusion in Cardiac Surgery: A Simulated Cost Reduction Model for Preoperative Anemia Management.

Acta medica portuguesa·2026
Same author

Evaluating visco-hyperelastic mechanical responses of hydrogel-based scaffolds and their potential for biomechanical restoration of the human mandibular joint.

Computers in biology and medicine·2025
Same author

Scalability of a graph neural network in accurate prediction of frictional contact networks in suspensions.

Soft matter·2025
Same author

Adhesion dynamics of Janus nanocarriers to endothelial cells: A dissipative particle dynamics study.

Physical review. E·2024
Same author

Adhesion dynamics of functionalized nanocarriers to endothelial cells: a dissipative particle dynamics study.

Soft matter·2023
Same author

The endocannabinoidome in human placenta: Possible contribution to the pathogenesis of preeclampsia.

BioFactors (Oxford, England)·2023

Related Experiment Video

Updated: Apr 9, 2026

Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
15:33

Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Published on: October 29, 2013

30.0K

PEGylation to Improve Protein Stability During Melt Processing.

Parker Lee1, Jenna Towslee1, João Maia1

  • 1Department of Macromolecular Science and Engineering, Case Western Reserve University, Cleveland, Ohio, 44106, USA.

Macromolecular Bioscience
|June 23, 2015
PubMed
Summary

PEGylation enhances protein stability during melt processing, improving lysozyme activity and dispersion. This method offers a promising solution for biopharmaceutical delivery systems, reducing activity loss and modifying drug release profiles.

Keywords:
PEGylationmelt processingpoly(lactic-co-glycolic acid)protein stability

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.4K
Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials
08:55

Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials

Published on: June 25, 2018

8.6K

Related Experiment Videos

Last Updated: Apr 9, 2026

Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
15:33

Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Published on: October 29, 2013

30.0K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.4K
Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials
08:55

Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials

Published on: June 25, 2018

8.6K

Area of Science:

  • Biopharmaceutical drug delivery
  • Polymer science
  • Protein stabilization

Background:

  • Biopharmaceuticals are effective but face delivery challenges.
  • Melt processing offers solvent-free, high-efficiency protein encapsulation.
  • Protein activity loss during melt processing due to heat and shear is a significant issue.

Purpose of the Study:

  • To investigate the impact of poly(ethylene glycol) or PEGylation on protein stability during melt processing.
  • To evaluate the effect of PEGylation on lysozyme activity and dispersion within poly(lactic-co-glycolic acid) or PLGA.
  • To assess PEGylation's influence on drug release kinetics in melt-processed systems.

Main Methods:

  • Utilized melt processing techniques for protein encapsulation.
  • Employed lysozyme as a model protein and PLGA as the matrix material.
  • Investigated the effects of covalent attachment of PEG (PEGylation) on protein properties.

Main Results:

  • PEGylation significantly increased the retained activity of lysozyme after melt processing.
  • Enhanced dispersion of lysozyme within the PLGA melt was observed with PEGylation.
  • The biphasic drug release profile typically seen in melt-processed systems was reduced by PEGylation.

Conclusions:

  • PEGylation is an effective strategy to enhance protein stability and activity during melt processing.
  • PEGylated proteins exhibit improved dispersion and modified release characteristics in PLGA-based systems.
  • This approach holds potential for developing more robust and effective biopharmaceutical delivery formulations.