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Peptide Bonds

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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: Feb 10, 2026

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Published on: December 6, 2017

Guiding principles for peptide nanotechnology through directed discovery.

A Lampel¹, R V Ulijn, T Tuttle

¹Advanced Science Research Center (ASRC) at the Graduate Center, City University of New York (CUNY), New York, NY, USA. lampelayala@gmail.com Rein.Ulijn@asrc.cuny.edu.

Chemical Society Reviews

|May 12, 2018

Summary

Scientists are designing novel nanoscale materials using the same simple amino acids found in nature. This research explores new methods to control material properties through peptide sequence design, creating functional systems without biological imitation.

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Area of Science:

Biochemistry
Materials Science
Nanotechnology

Background:

Life's functions rely on 20 canonical amino acids, which exhibit emergent properties when organized into complex 3D structures.
This review focuses on non-biological, directed discovery of functional nanoscale systems and materials.
Current approaches often mimic or modify existing biological systems.

Purpose of the Study:

To explore recent advancements in the directed discovery of functional nanoscale systems and materials.
To investigate sequence-structure relationships for assembly, reactivity, and complexation using amino acids.
To derive guiding principles for peptide sequence design in creating novel materials.

Main Methods:

Strategic editing of short peptide sequences to understand assembly.
Computational approaches for predicting and comparing peptide assembly behaviors.
Utilizing dynamic peptide libraries to explore the free energy landscape of assembly.

Main Results:

Insights into controlling order/disorder in peptide-based materials.
Understanding of how sequence design influences complexation and reactivity.
Development of guiding principles for creating functional nanoscale systems from amino acids.

Conclusions:

Peptide sequence design offers a powerful strategy for creating functional nanoscale systems and materials.
Complementary approaches reveal critical sequence-structure relationships.
This work provides a foundation for non-biological material design using fundamental building blocks.