Related Experiment Video
Updated: Jul 23, 2025

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
Published on: August 15, 2016
Influence of amino acid and N-terminal protection residue structures on peptide p-nitroanilide adsorption on
Alena V Kolesnichenko1, Nathalia A Kazmina1, Alexey A Chistov1
1Institute of Biomedical Chemistry, 10/8, Pogodinskaya ul., Moscow, 119121, Russia.
Abstract:
Polystyrene-based support Bio-Beads® SM-2 was employed for desalting peptide-p-nitroanilides from Oxone®. Neither tosyl, 9-fluorenyl(methoxycarbonyl), p-nitroanilide groups nor indolyl or p-hydroxyphenyl side-chains of Trp and Tyr ensured an efficient adsorption of peptide-p-nitroanilides onto Bio-Beads® SM-2. Only unsubstituted phenyl-containing protection groups (carbobenzoxy or benzoyl) and Phe residues provided the adsorption of peptides on Bio-Beads® SM-2 and their efficient desalting. This support is well suitable for multiple parallel phenyl group-containing peptide derivative separations and high-throughput screenings.
More Related Videos
Related Concept Videos
Basicity of Aromatic Amines
Structure of Amines
Basicity of Heterocyclic Aromatic Amines
Adrenergic Agonists: Chemistry and Structure-Activity Relationship
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of...
π Electron Effects on Chemical Shift: Overview
Basicity of Aliphatic Amines
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...

