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

Oral Hypoglycemic Agents: Glinides01:06

Oral Hypoglycemic Agents: Glinides

932
Repaglinide (Prandin) and Nateglinide (Starlix), known as glinides, are oral insulin secretagogues that stimulate insulin release from pancreatic β cells by closing the ATP-sensitive potassium channels (KATP channel). Repaglinide controls insulin release from pancreatic β cells by managing potassium efflux. It shares two binding sites with sulfonylureas and also has a unique site, indicating overlapping mechanisms of action. With a rapid onset and a 4-7 hour duration, it effectively...
932
Oral Hypoglycemic Agents: Biguanides and Glitazones01:26

Oral Hypoglycemic Agents: Biguanides and Glitazones

919
Biguanides, particularly metformin (Glucophage), are insulin sensitizers that enhance glucose uptake, thereby reducing insulin resistance. Unlike sulfonylureas, metformin doesn't prompt insulin secretion, which helps to curb hypoglycemia risk. Metformin is beneficial in treating conditions like polycystic ovary syndrome due to its insulin-resistance reduction capability. The drug's primary action involves curtailing hepatic gluconeogenesis, a significant contributor to high blood...
919
Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

1.0K
Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a...
1.0K
Glucagon-like Receptor Agonists01:24

Glucagon-like Receptor Agonists

1.3K
Incretins include glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which stimulate insulin secretion post-meals. In type 2 diabetes, GIP's efficacy is reduced, making GLP-1 a viable drug target. GIP originates from preproGIP.
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by...
1.3K
Antifungal Agents01:15

Antifungal Agents

37
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...
37
Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

1.9K
The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment...
1.9K

You might also read

Related Articles

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

Sort by
Same author

Bridging ancestry gaps in genomic risk prediction with tabular foundation models.

Bioinformatics (Oxford, England)·2026
Same author

<b>Lectotype designation for <i>Fowlea yunnanensis</i> (Anderson, 1879) (Squamata: Serpentes: Colubridae: Natricinae) and the first report of the species from India</b>.

Zootaxa·2026
Same author

<b>Redescription of a poorly known soft scale insect, <i>Pulvinaria ixorae</i> Green (Hemiptera: Coccomorpha: Coccidae) from India, with biological notes and a new distribution record</b>.

Zootaxa·2026
Same author

<b>Designation of a lectotype for <i>Trimeresurus porphyraceus</i> Blyth, 1861 (Reptilia: Viperidae) and its recognition as a junior synonym of <i>Trimeresurus erythrurus</i> (Cantor, 1839)</b>.

Zootaxa·2026
Same author

BRAF Inhibition in Congenital Nevi and Neural Melanosis.

JAMA dermatology·2026
Same author

The impact of international care networks on the clinical management of constitutional mismatch repair deficiency (CMMRD): a review of recent developments.

Familial cancer·2026

Related Experiment Video

Updated: Mar 27, 2026

An In Ovo Model for Testing Insulin-mimetic Compounds
06:09

An In Ovo Model for Testing Insulin-mimetic Compounds

Published on: April 23, 2018

11.2K

Repurposing an Antifungal Drug as an Effective Insulin Aggregation Inhibitor.

Anirban Das1, Nihar Ranjan Dalabehera1, Suman Pahal2

  • 1Department of Chemistry, Indian Institute of Science Education and Research Bhopal, Bhopal, Madhya Pradesh, India.

Chemistry, an Asian Journal
|March 24, 2026
PubMed
Summary

An antifungal drug, Nystatin, prevents insulin aggregation, maintaining its stability and efficacy for diabetes management. This repurposed drug ensures soluble, non-toxic insulin formulations that effectively control blood sugar.

Keywords:
aggregationdrug repurposinginhibitorsinsulininsulin bioactivity

More Related Videos

Homogeneous Time-resolved F&#246;rster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
07:30

Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion

Published on: May 10, 2018

9.8K
Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications
09:39

Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications

Published on: February 7, 2021

9.2K

Related Experiment Videos

Last Updated: Mar 27, 2026

An In Ovo Model for Testing Insulin-mimetic Compounds
06:09

An In Ovo Model for Testing Insulin-mimetic Compounds

Published on: April 23, 2018

11.2K
Homogeneous Time-resolved F&#246;rster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
07:30

Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion

Published on: May 10, 2018

9.8K
Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications
09:39

Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications

Published on: February 7, 2021

9.2K

Area of Science:

  • Biochemistry
  • Pharmacology
  • Drug Repurposing

Background:

  • Recombinant insulin is crucial for diabetes management but prone to aggregation during storage and transport, compromising glycemic control.
  • Insulin aggregation reduces therapeutic efficacy and poses challenges for long-term stability of insulin formulations.

Purpose of the Study:

  • To identify an existing drug capable of preventing insulin aggregation and maintaining insulin's therapeutic properties.
  • To evaluate the efficacy of repurposed Nystatin in preventing insulin fibrillation and preserving its function.

Main Methods:

  • Virtual screening of 5500 FDA-approved drugs to identify potential insulin aggregation inhibitors.
  • In vitro assessment of Nystatin's effect on insulin solubility, secondary structure, and cell toxicity.
  • Evaluation of Nystatin-treated insulin formulations (Aspart, Lispro, Glargine) for insulin receptor activation and in vivo glycemic control in a diabetic rat model.

Main Results:

  • Nystatin effectively inhibited insulin aggregation under physiological conditions, maintaining complete solubility and native secondary structure.
  • Nystatin treatment did not induce toxicity in HEK293T cells and preserved the insulin formulations' ability to activate the insulin receptor.
  • Nystatin successfully prevented fibrillation in fast-acting (Aspart, Lispro) and slow-acting (Glargine) insulin formulations, demonstrating efficacy in a diabetic rat model for glycemic control.

Conclusions:

  • Repurposed Nystatin is a potent inhibitor of insulin aggregation, offering a promising strategy for stabilizing insulin formulations.
  • Nystatin maintains insulin's structural integrity, bioactivity, and therapeutic efficacy, with potential for use in commercial insulin products.
  • This study highlights the potential of drug repurposing to address critical challenges in pharmaceutical stability and drug delivery for chronic diseases like diabetes.