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

Basicity of Heterocyclic Aromatic Amines

Basicity of Heterocyclic Aromatic Amines

Heterocyclic amines, where the N atom is a part of an alicyclic system, are similar in basicity to alkylamines. Interestingly, the heterocyclic amine having a nitrogen atom as part of an aromatic ring has much less basicity than its corresponding alicyclic counterpart. For this reason, as presented in Figure 1, piperidine (pKb = 2.8) is significantly more basic than pyridine (pKb = 8.8).

Factors Affecting Protein-Drug Binding: Drug Interactions

Factors Affecting Protein-Drug Binding: Drug Interactions

Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Basicity of Aliphatic Amines

Basicity of Aliphatic Amines

Amines can behave as Brønsted–Lowry bases by accepting a proton from the acid to form corresponding conjugate acids. Due to a lone pair of nonbonding electrons, aliphatic amines can also act as Lewis bases by forming a covalent bond with an electrophile.
To measure the basicity of amines, two conventions are generally used. The first defines Kb as the basicity constant for the deprotonation reaction of water by the amine, as presented in Figure 1. Conventionally, lower Kb indicates higher...

Basicity of Aromatic Amines

Basicity of Aromatic Amines

The basicity of aromatic amines is much weaker than that of aliphatic amines due to the involvement of the lone pair of electrons over the N atom in resonance with the aryl rings. Generally, the electron-donating ability of any substituents on the aryl ring of aromatic amines increases the basicity of the amine by increasing electron density, and hence the availability of lone pair on the nitrogen. On the other hand, electron-withdrawing functional groups on the aryl ring of amines decrease the...

Ionic Strength: Effects on Chemical Equilibria

Ionic Strength: Effects on Chemical Equilibria

The addition of an inert ionic compound increases the solubility of a sparingly soluble salt. For example, adding potassium nitrate to a saturated solution of calcium sulfate significantly enhances the solubility of calcium sulfate. Le Châtelier's principle cannot predict this shift in the equilibrium. Instead, this could be explained in terms of changes in the effective concentration of the ions in solution in the presence of added inert salt.
In this solution, the primary...

You might also read

Related Articles

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

Sort by

Same author

Phage-Functionalized Magnetic Separation for Rapid and Selective Detection of <i>Escherichia coli</i>.

ACS omega·2026

Same author

Structural dynamics in the CENP-A nucleosome impacted by protein-protein interactions with centromere protein N.

Nanoscale·2026

Same author

Luminescent Copper(I) Complexes with Dual Bridging Ligands and Excitation-Dependent Emission.

Inorganic chemistry·2026

Same author

Polymer-Coated Iron Oxide Nanoparticles as an Effective Tool for Histamine Extraction: Synthesis, Characterization, and Application.

ACS omega·2026

Same author

Influence of coprecipitation synthesis parameters on the physicochemical properties and biological effects of iron oxide nanoparticles.

Nanoscale advances·2025

Same author

Bio Meets Nano: Protein Exchange in Saline Biocoronae on Magnetic Nanoparticles.

International journal of molecular sciences·2025

Search research articles

Related Experiment Video

Updated: Dec 12, 2025

Preparation of Functional Silica Using a Bioinspired Method

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Buffer Influence on the Amino Acid Silica Interaction.

Saientan Bag¹, Stefan Rauwolf², Mikhail Suyetin¹

¹Institute of Nanotechnology (INT), Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry

|August 15, 2020

Summary

Buffer type significantly impacts protein-surface interactions, crucial for biotechnology. Arginine and lysine show strong silica binding, with buffer pH altering affinity differently for MOPS and TRIS buffers.

Keywords:

amino acids buffer chromatography multiscale modelling of adsorption silica

More Related Videos

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts

Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts

Published on: April 13, 2022

Related Experiment Videos

Last Updated: Dec 12, 2025

Preparation of Functional Silica Using a Bioinspired Method

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts

Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts

Published on: April 13, 2022

Area of Science:

Biochemistry
Materials Science
Biotechnology

Background:

Protein-surface interactions are vital in life sciences and biotechnology.
Buffer systems are commonly used but their influence on these interactions is understudied.

Purpose of the Study:

To systematically investigate the impact of buffer type and pH on protein-surface interactions.
To understand the binding mechanisms of amino acids to silica surfaces.

Main Methods:

Chromatographic experiments to measure amino acid-silica interactions.
Free energy calculations to validate binding affinities.
Multiscale modeling combining molecular dynamics and Langmuir adsorption models.

Main Results:

Arginine (R) and lysine (K) exhibit the strongest binding to silica among 20 proteinogenic amino acids.
The binding affinity of R/K to silica shows opposite trends with pH in MOPS and TRIS buffers.
Experimental findings are supported by theoretical free energy calculations.

Conclusions:

Buffer composition and pH critically influence protein-surface interactions.
Understanding these effects allows for optimization of buffer conditions in biosensors, drug delivery, and bioseparation.
Multiscale modeling provides a predictive framework for optimizing experimental conditions.