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

Drug Distribution: Plasma Protein Binding

Drug Distribution: Plasma Protein Binding

Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...

Protein-Drug Binding: Mechanism and Kinetics

Protein-Drug Binding: Mechanism and Kinetics

Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...

Hepatic Drug Clearance: Effect of Protein Binding

Hepatic Drug Clearance: Effect of Protein Binding

Hepatic clearance is influenced by protein binding based on the drug's extraction ratio. Drugs with high extraction ratios are considered flow-limited and remain unaffected by protein binding during hepatic clearance. On the other hand, drugs with low extraction ratios may be impacted by plasma protein binding, although the extent of this influence depends on the fraction of the drug bound.
For low-extraction-ratio drugs that are less than 80% protein-bound, minor changes in protein binding...

Estimation of k and VD of Aminoglycosides

Estimation of k and V_D of Aminoglycosides

Aminoglycosides are a class of antibiotics used to treat various bacterial infections. Clinicians must determine the elimination rate constant (k) and volume of distribution (VD) to optimize therapeutic efficacy and minimize toxicity. The k value represents the rate at which the drug is removed from the body, and the VD reflects the degree to which the drug distributes into body tissues. Accurately estimating these parameters allows healthcare professionals to tailor drug dosing to individual...

Inhibitors of Gram-positive Cell Wall Synthesis

Inhibitors of Gram-positive Cell Wall Synthesis

Bacterial cell walls are typically rigid structures composed mainly of peptidoglycan, a mesh-like polymer that provides mechanical strength and maintains cell shape. The synthesis of peptidoglycan is a crucial process in bacterial growth and serves as a primary target for many antibiotics.Mechanism of Action of Beta-Lactam AntibioticsBeta-lactam antibiotics, such as penicillin, inhibit peptidoglycan synthesis in actively growing cells. These antibiotics share a characteristic four-membered...

You might also read

Related Articles

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

Sort by

Same author

Precise Spectroscopy of the 3n and 3p Systems via the ^{3}H(t, ^{3}He)3n and ^{3}He(^{3}He, t)3p Reactions at Intermediate Energies.

Physical review letters·2024

Same author

In-process monitoring of a tissue-engineered oral mucosa fabricated on a micropatterned collagen scaffold: use of optical coherence tomography for quality control.

Heliyon·2022

Same author

Cross-Sectional Inverse Association of Regular Soy Intake with Insulin Resistance in Japanese Elderly.

Journal of nutrition in gerontology and geriatrics·2018

Same author

Aeromonas enteritis: a great mimicker of acute appendicitis.

QJM : monthly journal of the Association of Physicians·2018

Same author

Intestinal amoebiasis in a patient with acute graft-versus-host disease after allogeneic bone marrow transplantation successfully treated by metronidazole.

Transplant infectious disease : an official journal of the Transplantation Society·2015

Same author

Presence of autoimmune regulator and absence of desmoglein 1 in a thymoma in a patient with pemphigus foliaceus.

The British journal of dermatology·2014

Search research articles

Related Experiment Video

Updated: Jul 23, 2026

Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection

Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection

Published on: October 25, 2013

Adherence of vancomycin to proteins.

K Kishimoto¹, J M Manning

¹Department of Biology, Northeastern University, Boston, MA 02115, USA.

Journal of Protein Chemistry

|January 5, 2002

Summary

Vancomycin can cause protein aggregation and self-binding (dimerization), potentially linked to its antimicrobial effects. Researchers developed methods to measure these properties, revealing anion influence on both processes.

Area of Science:

Biochemistry
Microbiology
Spectroscopy

Background:

Vancomycin exhibits unique protein-binding properties, including self-aggregation (dimerization) and promotion of protein aggregation.
These molecular interactions are hypothesized to contribute to vancomycin's antimicrobial efficacy.
Quantifying these properties is crucial for understanding vancomycin's mechanism of action.

Purpose of the Study:

To establish reliable methods for measuring vancomycin's dimerization and protein aggregation.
To investigate the relationship between vancomycin's dimerization, protein aggregation, and anion presence.
To correlate these molecular behaviors with vancomycin's antimicrobial activity.

Main Methods:

Near-ultraviolet circular dichroism (CD) spectroscopy was employed to determine the vancomycin monomer-dimer equilibrium constant.

More Related Videos

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance

Published on: October 16, 2018

A Novel Method to Determine the Longitudinal Antibacterial Activity of Drug-Eluting Materials

A Novel Method to Determine the Longitudinal Antibacterial Activity of Drug-Eluting Materials

Published on: March 3, 2023

Related Experiment Videos

Last Updated: Jul 23, 2026

Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection

Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection

Published on: October 25, 2013

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance

Published on: October 16, 2018

A Novel Method to Determine the Longitudinal Antibacterial Activity of Drug-Eluting Materials

A Novel Method to Determine the Longitudinal Antibacterial Activity of Drug-Eluting Materials

Published on: March 3, 2023

High-resolution gel filtration was used as a complementary method for measuring dimerization.

Turbidity measurements assessed the aggregation of purified proteins induced by vancomycin.

Main Results:

Circular dichroism spectral shifts in vancomycin monomers allowed for the determination of the monomer-dimer equilibrium constant.
Both vancomycin dimerization and protein aggregation were found to be influenced by anions.
The effectiveness of anions in modulating these processes correlated with their carboxyl pKa values.

Conclusions:

Established spectroscopic and chromatographic methods accurately quantify vancomycin dimerization.
Vancomycin-induced protein aggregation and self-dimerization are anion-dependent processes.
The observed anion influence provides a mechanistic link between vancomycin's molecular interactions and its biological activity.