Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

72
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
72
Peptide Bonds02:43

Peptide Bonds

74.9K
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...
74.9K
What are Proteins?01:28

What are Proteins?

14.8K
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
14.8K
Amino acids03:42

Amino acids

89.3K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
89.3K
Protein Organization01:24

Protein Organization

6.6K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.6K
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

43
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
43

You might also read

Related Articles

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

Sort by
Same author

Amino-functionalized bimetallic MOF nanozyme <i>via</i> solvent-assisted ligand exchange for interference-free phenolic detection.

Analytical methods : advancing methods and applications·2026
Same author

Why covalent organic frameworks grow twisted on graphite.

Nature communications·2025
Same author

POM-Based Water Splitting Catalyst Under Acid Conditions Driven by Its Assembly on Carbon Nanotubes.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

Polyimide-Linked Hexaazatriphenylene-Based Porous Organic Polymer with Multiple Redox-Active Sites as a High-Capacity Organic Cathode for Lithium-Ion Batteries.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

The Versatility of NADES Across Applications.

Molecules (Basel, Switzerland)·2025

Related Experiment Video

Updated: Jul 25, 2025

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

18.2K

Non-Canonical Amino Acids as Building Blocks for Peptidomimetics: Structure, Function, and Applications.

Tarsila G Castro1,2, Manuel Melle-Franco3, Cristina E A Sousa4

  • 1CEB-Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.

Biomolecules
|June 28, 2023
PubMed
Summary

Non-canonical amino acids enhance peptide stability and function. This review classifies these unique residues and their use in designing novel peptidomimetics for new molecules and materials.

Keywords:
backbone modificationsfoldamersnon-canonical amino acidspeptidomimeticsside-chain modificationsstructure-function relationship

More Related Videos

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

29.5K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.4K

Related Experiment Videos

Last Updated: Jul 25, 2025

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

18.2K
Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

29.5K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.4K

Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Medicinal Chemistry

Background:

  • Non-canonical amino acids (ncAAs) are prevalent in nature, influencing peptide stability and biological activity.
  • Unlike standard amino acids, the structural and functional roles of ncAAs are not fully elucidated.
  • This review focuses on ncAAs and their application in peptidomimetic design.

Purpose of the Study:

  • To provide an overview of non-canonical amino acids.
  • To classify ncAAs based on their ability to induce secondary structures and enhance stability.
  • To explore the application of ncAAs in peptidomimetics.

Main Methods:

  • Compilation of experimental and molecular modeling data.
  • Classification of ncAAs based on structural modifications (side-chain and backbone).
  • Review of specific ncAAs including dialkyl glycines, cyclized amino acids, proline analogues, and dehydro amino acids.

Main Results:

  • Identified various classes of ncAAs with distinct structural and functional properties.
  • Demonstrated that ncAAs can induce specific secondary structures, improving peptide stability.
  • Highlighted backbone modifications like retro-inverso peptidomimetics and depsipeptides.

Conclusions:

  • Non-canonical amino acids are crucial for enhancing peptide stability and biological function.
  • Understanding ncAAs facilitates the design of advanced peptidomimetics.
  • Peptidomimetics derived from ncAAs hold promise for developing new therapeutics and materials.