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

Antifungal Agents01:15

Antifungal Agents

Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to cholesterol contributes to...

You might also read

Related Articles

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

Sort by
Same author

Enzymatic Biocontrol of Fire Blight (<i>Erwinia amylovora</i>) Using an Engineered Glycosyl Hydrolase.

Environmental science & technology·2026
Same author

Enzyme-enhanced RNA isolation from biofilm-producing bacteria.

Microbiology spectrum·2026
Same author

Optimizing Scaled up Production and Purification of Recombinant Hydrophobin HFBI in <i>Pichia pastoris</i>.

Microorganisms·2025
Same author

Directed Evolution of Silicatein Reveals Biomineralization Synergism between Protein Sequences.

ACS omega·2025
Same author

Applying a polysaccharide lyase from <i>Stenotrophomonas maltophilia</i> to disrupt alginate exopolysaccharide produced by <i>Pseudomonas aeruginosa</i> clinical isolates.

Applied and environmental microbiology·2024
Same author

High-Speed Imaging-Based Particle Attribute Analysis of Spray-Dried Amorphous Solid Dispersions Using a Convolution Neural Network.

Molecular pharmaceutics·2024

Related Experiment Video

Updated: Jun 21, 2026

Flash NanoPrecipitation for the Encapsulation of Hydrophobic and Hydrophilic Compounds in Polymeric Nanoparticles
10:12

Flash NanoPrecipitation for the Encapsulation of Hydrophobic and Hydrophilic Compounds in Polymeric Nanoparticles

Published on: January 7, 2019

22.6K

Engineered Hydrophobin as a Crystallization Inhibitor for Flufenamic Acid.

Nathanael Sallada1, Yongjun Li2, Bryan Berger1,3

  • 1Department of Biomedical Engineering, University of Virginia, Charlottesville, Virginia 22904, United States.

ACS Applied Bio Materials
|January 10, 2022
PubMed
Summary

Engineered hydrophobins (HFB1) show superior performance as crystallization inhibitors compared to common polymers. This finding supports their use in amorphous drug delivery systems for enhanced drug solubility and stability.

Keywords:
crystallizationcrystallization inhibitionhydrophobinprecipitationsupersaturation

More Related Videos

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

24.3K
A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization
08:01

A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization

Published on: August 18, 2022

3.2K

Related Experiment Videos

Last Updated: Jun 21, 2026

Flash NanoPrecipitation for the Encapsulation of Hydrophobic and Hydrophilic Compounds in Polymeric Nanoparticles
10:12

Flash NanoPrecipitation for the Encapsulation of Hydrophobic and Hydrophilic Compounds in Polymeric Nanoparticles

Published on: January 7, 2019

22.6K
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

24.3K
A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization
08:01

A Microfluidic Approach for the Study of Ice and Clathrate Hydrate Crystallization

Published on: August 18, 2022

3.2K

Area of Science:

  • Biochemistry
  • Materials Science
  • Pharmaceutical Sciences

Background:

  • Hydrophobins are highly surface-active proteins from fungi with diverse applications.
  • Their properties make them suitable for drug delivery, protein purification, and biomaterial development.
  • Engineered hydrophobins offer potential for advanced pharmaceutical formulations.

Purpose of the Study:

  • To evaluate an engineered hydrophobin (HFB1) as a crystallization inhibitor for amorphous drug delivery.
  • To compare HFB1's efficacy against established polymeric crystallization inhibitors.
  • To elucidate the mechanism of crystallization inhibition by HFB1.

Main Methods:

  • Utilized a supersaturation-precipitation method with UV fiber optic monitoring.
  • Employed flufenamic acid (FA) as a model drug due to its poor aqueous solubility.
  • Compared HFB1 with pharmaceutical polymers: Methocel (A4C, K15M), Kollidon VA64, and HPMCAS (MF).
  • Analyzed results using Dynamic Light Scattering (DLS) and Circular Dichroism (CD).

Main Results:

  • HFB1 demonstrated superior crystallization inhibition compared to all tested polymers.
  • HFB1 was effective at significantly lower concentrations than polymeric inhibitors.
  • DLS and CD data suggest a unique inhibition mechanism dependent on drug phase.

Conclusions:

  • Engineered hydrophobins (HFB1) are highly effective crystallization inhibitors for amorphous drug delivery systems.
  • HFB1 offers a promising alternative to conventional polymers, enabling lower usage concentrations.
  • Understanding HFB1's mechanism can optimize its application in stabilizing supersaturated drug solutions.