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Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Related Experiment Video

Updated: May 13, 2026

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Published on: August 15, 2016

Structural attributes affecting peptide entrapment in PEO brush layers.

Marsha C Lampi¹, Xiangming Wu, Karl F Schilke

¹School of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331, USA.

Colloids and Surfaces. B, Biointerfaces

|February 26, 2013

Summary

Understanding peptide interactions with polyethylene oxide (PEO) brush layers is key for drug delivery. Peptide structure and amphiphilicity influence loading and release, enabling new anti-fouling coatings for therapeutics.

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Published on: October 29, 2013

Area of Science:

Biomaterials Science
Surface Chemistry
Drug Delivery Systems

Background:

Developing effective drug storage and delivery systems requires a quantitative understanding of peptide interactions with surface coatings.
Polyethylene oxide (PEO) brush layers are promising for anti-fouling applications but their peptide interaction dynamics need further elucidation.

Purpose of the Study:

To investigate the impact of peptide structure and amphiphilicity on adsorption and desorption kinetics within PEO brush layers.
To establish a foundation for designing advanced anti-fouling coatings for therapeutic applications.

Main Methods:

Utilized Optical Waveguide Lightmode Spectroscopy (OWLS) and Circular Dichroism (CD) to analyze peptide adsorption.
Characterized adsorption and desorption kinetics of poly-l-glutamic acid, poly-l-lysine, and WLBU2 peptide.
Employed a model for protein adsorption to determine rate constants for loosely and tightly bound states.

Main Results:

Peptide structure (disordered vs. ordered/helical) influenced adsorption and elution rates.
Peptide amphiphilicity was critical for determining resistance to elution from the PEO layer.
Kinetic patterns revealed distinct adsorption and desorption behaviors based on peptide properties.

Conclusions:

Peptide structure and amphiphilicity are critical parameters for controlling peptide loading and release from PEO brush layers.
These findings support the potential of PEO brush coatings as tunable platforms for anti-fouling surfaces and therapeutic delivery.
The study provides quantitative insights into peptide-surface interactions for advanced biomaterial design.