Related Experiment Video

Updated: Aug 14, 2026

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Developments in the design and synthesis of calpain inhibitors

Axel T Neffe1, Andrew D Abell

  • 1University of Canterbury, Department of Chemistry, Christchurch 8020, New Zealand. axel.neffe@canterbury.ac.nz

Current Opinion in Drug Discovery & Development
|November 30, 2005
PubMed

Insights

Calpains, crucial Ca(2+)-dependent proteases, are implicated in diseases. This review details calpain structures and novel inhibitors, aiding drug development for conditions like cataracts and brain injury.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Calpains are calcium-dependent cysteine proteases vital for cell differentiation and death.
  • Overactivated calpain is linked to diseases such as cataracts and traumatic brain injury.
  • Developing selective calpain inhibitors is challenging due to limited structural data.

Purpose of the Study:

  • To review the properties and X-ray crystal structures of calpains.
  • To discuss the synthesis and binding affinities of novel calpain inhibitors.
  • To provide insights for developing targeted calpain-modulating therapies.

Main Methods:

  • Analysis of existing X-ray crystal structures of engineered calpains.
  • Biochemical characterization of calpain properties.
  • Synthesis and evaluation of novel calpain inhibitor compounds.

Main Results:

  • Recent structural data and biochemical characterization have improved understanding of calpain.
  • Novel calpain inhibitors have been synthesized with characterized binding affinities.
  • The review consolidates current knowledge on calpain structure-activity relationships.

Conclusions:

  • Advances in calpain structural biology and inhibitor development offer new therapeutic avenues.
  • Targeting calpain effectively requires detailed structural and biochemical insights.
  • This review serves as a resource for researchers in calpain-related disease and drug discovery.

More Related Videos

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...