Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Ribozymes

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...

Ribozymes

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...

Drug toxicity: Drug–Drug Interaction

Drug toxicity: Drug–Drug Interaction

Drug–drug interactions can precipitate toxicity through multiple mechanisms. Absorption interactions alter how drugs enter the body, exemplified when ranitidine increases the absorption of basic drugs, while cholestyramine decreases the levels of propranolol. Protein binding interactions occur when drugs share the same binding sites on plasma proteins. Drugs like aspirin and warfarin, when bound in excess, can lead to increased free drug concentrations, enhancing the potential for...

Riboswitches

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...

Types of RNA

Types of RNA

Overview
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...

Types of RNA

Types of RNA

Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in regulating gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA Performs Diverse...

You might also read

Related Articles

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

Sort by

Same author

DNA acidification by citric acid and gallic acid: acid binding site and DNA structural dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Locating the binding sites of citric acid and gallic acid on milk <i>β</i>-lactoglobulin.

Journal of biomolecular structure & dynamics·2020

Same author

A computational exploration into the structure, antioxidant capacity, toxicity and drug-like activity of the anthocyanidin "Petunidin".

Heliyon·2020

Same author

Binding efficacy of aminobenzoic acid derivatives with DNA duplex: drug binding sites and DNA structure and dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis.

Journal of biomolecular structure & dynamics·2020

Same author

Application and biomolecular study of functionalized folic acid-dendrimer nanoparticles in drug delivery.

Journal of biomolecular structure & dynamics·2020

Search research articles

Related Experiment Video

Updated: Jul 20, 2026

NMR-Based Activity Assays for Determining Compound Inhibition, IC50 Values, Artifactual Activity, and Whole-Cell Activity of Nucleoside Ribohydrolases

NMR-Based Activity Assays for Determining Compound Inhibition, IC₅₀ Values, Artifactual Activity, and Whole-Cell Activity of Nucleoside Ribohydrolases

Published on: June 30, 2019

Aspirin interaction with ribonuclease A.

J F Neault¹, C Ragi, A Novetta-Dellen

¹Department of Chemistry-Biology, University of Québec at Trois-Rivières, C.P. 500, Trois-Rivières (Québec) Canada G9A 5H7.

Cell Biochemistry and Biophysics

|September 1, 2006

Summary

Aspirin binds to Ribonuclease A (RNase A) with a binding constant of 3.57 x 10(4) M-1. This interaction causes minor unfolding of the RNase A protein structure.

Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Aspirin, an anti-inflammatory drug, is known to cause protein acetylation, altering protein function.
Ribonuclease A (RNase A) possesses multiple high-affinity binding sites, making it a potential target for various molecules.
Understanding drug-protein interactions is crucial for drug development and predicting therapeutic effects.

Purpose of the Study:

To investigate the interaction between aspirin and Ribonuclease A (RNase A) under physiological conditions.
To determine the binding mode and binding constant of aspirin to RNase A.
To assess the conformational changes in RNase A upon complexation with aspirin.

Main Methods:

Ultraviolet-visible (UV-Vis) spectroscopy

More Related Videos

Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NFκB Activity and Breast Cancer Stem Cells

Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NFκB Activity and Breast Cancer Stem Cells

Published on: January 18, 2017

Related Experiment Videos

Last Updated: Jul 20, 2026

NMR-Based Activity Assays for Determining Compound Inhibition, IC50 Values, Artifactual Activity, and Whole-Cell Activity of Nucleoside Ribohydrolases

NMR-Based Activity Assays for Determining Compound Inhibition, IC₅₀ Values, Artifactual Activity, and Whole-Cell Activity of Nucleoside Ribohydrolases

Published on: June 30, 2019

Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NFκB Activity and Breast Cancer Stem Cells

Synthesis and Characterization of an Aspirin-fumarate Prodrug that Inhibits NFκB Activity and Breast Cancer Stem Cells

Published on: January 18, 2017

Fourier transform infrared (FTIR) spectroscopy

Circular dichroism (CD) spectroscopy

Analysis of protein conformational changes using CDPro program

Main Results:

Spectroscopic analysis revealed a primary binding interaction between aspirin and RNase A.
The overall binding constant (K) for the aspirin-RNase A complex was determined to be 3.57 x 10(4) M-1.
A minor reduction in the protein's alpha-helix content was observed, from 15.5% to 14.1% (CD) and 26% to 21% (FTIR), indicating partial protein unfolding.

Conclusions:

Aspirin forms a complex with RNase A, characterized by a specific binding constant.
The interaction leads to subtle alterations in RNase A's secondary structure, suggesting a degree of protein unfolding.
These findings provide insights into the molecular interactions between aspirin and proteins, relevant for understanding drug mechanisms.