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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...

Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Updated: Oct 26, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

From structure to application: Progress and opportunities in peptide materials development.

Tania L Lopez-Silva¹, Joel P Schneider¹

¹Chemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, United States.

Current Opinion in Chemical Biology

|July 30, 2021

Summary

This summary is machine-generated.

Peptide materials show promise in biomedicine, but structural characterization and biological interactions require further research for clinical translation. Understanding these peptide assemblies is key to advancing applications like drug delivery and tissue regeneration.

Keywords:

Assembling peptides Biological responses to peptide materials Drug delivery Peptide fibril structure Peptide-based materials

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Last Updated: Oct 26, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

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Published on: February 27, 2019

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

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Published on: January 26, 2016

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Area of Science:

Biomaterials Science
Biomedical Engineering
Molecular Biology

Background:

Peptide materials, including hydrogels and fibrils, have been utilized in biomedical applications for over two decades.
Despite widespread use, their structural characterization lags behind that of amyloid proteins.
Key research areas, such as structural features guiding assembly and biological interactions, remain underexplored.

Purpose of the Study:

To examine structural motifs in peptide designs that drive self-assembly and confer specificity.
To highlight the need for advanced structural characterization of peptide assemblies, mirroring the progress in amyloid proteins.
To underscore the importance of understanding peptide material interactions with biological systems for clinical translation.

Main Methods:

Review and analysis of existing literature on peptide material design and structural characterization.
Examination of common interactions driving self-assembly in peptide-based materials.
Synthesis of current knowledge on biological responses to peptide materials.

Main Results:

Identified common interactions and structural motifs crucial for peptide assembly and specificity.
Highlighted a gap in atomic-resolution structural characterization of designed peptide assemblies compared to amyloid proteins.
Revealed limited understanding of fundamental interactions between peptide materials and biological systems (cells, immune system).

Conclusions:

Further structural characterization of peptide assemblies is essential to validate design principles.
A deeper understanding of peptide material interactions with biological systems is critical for successful clinical translation.
Investigating how material properties influence biological responses will accelerate the development of peptide-based therapeutics and regenerative medicine.