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

Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones01:24

Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones

4.9K
Acetals are formed by reacting two equivalents of alcohol with carbonyl compounds like aldehydes or ketones. Acetals are unaffected by bases, nucleophiles, oxidizing agents, and reducing agents. They serve as protecting groups for aldehydes and ketones. Acetals can be easily formed and also easily removed via mild acid hydrolysis.
In the presence of multiple functional groups, when selective reduction of one group over the other is desired, groups like aldehydes and ketones that form acetals...
4.9K
Protecting Groups for Aldehydes and Ketones: Introduction01:23

Protecting Groups for Aldehydes and Ketones: Introduction

8.1K
Protecting groups are compounds that can bind to a specific functional group in the presence of other functional groups to protect them from undesired chemical reactions. These compounds can selectively bind to particular functional groups and advance chemoselective reactions in polyfunctional systems (Figure 1). After the functional group has served its purpose, it is removed by reacting it with specific compounds.
8.1K
Enzyme Inhibition01:30

Enzyme Inhibition

86.1K
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
86.1K
Masking and Demasking Agents01:19

Masking and Demasking Agents

2.9K
EDTA titrations may necessitate masking and demasking agents to temporarily protect a particular metal ion in a mixture from the EDTA reaction. These agents facilitate the sequential analysis of the metal ions by forming stable complexes with some—but not all—metal ions during certain steps.
There are many masking agents, such as cyanide, fluoride, triethanolamine, thiourea, and 2,3-bis(sulfanyl)propan-1-ol (formerly 2,3-dimercapto-1-propanol), with the masking agent chosen based on...
2.9K
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

2.1K
Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
2.1K
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:29

Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

726
Indirect-acting cholinergic agonists are agents that interact with the acetylcholinesterase enzyme in the synaptic cleft, preventing the breakdown of acetylcholine into choline and acetate. Consequently, the concentration of acetylcholine in the synaptic cleft increases. These agonists can be classified into reversible and irreversible inhibitors based on their duration of action.
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
726

You might also read

Related Articles

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

Sort by
Same author

Substrate Specificity and Kinetic Mechanism of the NAD<sup>+</sup>-Dependent Deacylase from <i>Mycobacterium tuberculosis</i>, Rv1151c (<i>Mt</i>-Sirt).

Biochemistry·2026
Same author

Incorporation of Butyryl-Lysine into Phage-Displayed Peptide Libraries.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Advances in deciphering intratumoral versus peritumoral heterogeneity of infiltrating lymphocytes in pancreatic cancer: a spatial perspective.

Translational oncology·2026
Same author

Disulfide bond formation between Cys22 and Cys44 in SARS-CoV-2 main protease.

Bioorganic & medicinal chemistry letters·2026
Same author

Temperature and lipid composition differentially regulate KRAS assemblies on membranes.

Chemical communications (Cambridge, England)·2026
Same author

Harmonizing Peak Matching Between Multidimensional NMR Spectra.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Oct 27, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.8K

Self-Masked Aldehyde Inhibitors: A Novel Strategy for Inhibiting Cysteine Proteases.

Linfeng Li1, Bala C Chenna1, Kai S Yang2

  • 1Department of Biochemistry and Biophysics, Texas A&M University, 300 Olsen Blvd, College Station, Texas 77843, United States.

Journal of Medicinal Chemistry
|July 21, 2021
PubMed
Summary

Novel self-masked aldehyde inhibitors (SMAIs) offer potent, reversible inhibition of cruzain, a key target in Chagas disease. This approach addresses safety and stability concerns associated with traditional aldehyde inhibitors.

More Related Videos

Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

12.8K
Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology
10:25

Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology

Published on: November 22, 2024

428

Related Experiment Videos

Last Updated: Oct 27, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

6.8K
Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

12.8K
Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology
10:25

Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology

Published on: November 22, 2024

428

Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Parasitology

Background:

  • Cysteine proteases are critical drug targets for infectious diseases like Chagas disease (cruzain) and COVID-19 (3CL protease, cathepsin L).
  • Peptide aldehydes are effective inhibitors but face challenges due to safety concerns and metabolic instability.
  • The high electrophilicity of aldehyde groups limits their therapeutic application.

Purpose of the Study:

  • To develop a novel class of self-masked aldehyde inhibitors (SMAIs) targeting cruzain, the primary cysteine protease of *Trypanosoma cruzi*.
  • To evaluate the potency, reversibility, and cell-based efficacy of SMAIs against cruzain.
  • To explore the potential of SMAIs as a therapeutic strategy for Chagas disease and other protease-mediated conditions, including COVID-19.

Main Methods:

  • Design and synthesis of novel self-masked aldehyde inhibitors (SMAIs).
  • Enzymatic assays to determine inhibitory constants (K*) and assess reversibility against cruzain.
  • Cell-based assays to evaluate inhibitor efficacy and aldehyde protection.
  • Kinetic and chemical mechanism elucidation of SMAI inhibition.
  • Application of the SMAI strategy to design inhibitors for SARS-CoV-2 3CL protease.

Main Results:

  • SMAIs demonstrated potent and reversible inhibition of cruzain with K* values ranging from 18-350 nM.
  • SMAIs appeared to protect the aldehyde moiety in cell-based assays, mitigating potential toxicity.
  • Prodrugs of SMAIs were synthesized to enhance pharmacokinetic properties.
  • The kinetic and chemical mechanisms of SMAI action were successfully elucidated.
  • The SMAI strategy was successfully applied to the design of anti-SARS-CoV-2 inhibitors.

Conclusions:

  • Self-masked aldehyde inhibitors (SMAIs) represent a promising new class of potent and reversible cruzain inhibitors.
  • SMAIs overcome the limitations of traditional aldehyde inhibitors, offering improved safety and stability profiles.
  • This strategy holds significant potential for developing new therapeutics against Chagas disease and viral infections like COVID-19.