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Related Concept Videos

Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

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 biosynthesis begins in...
Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
Peptide Bonds02:43

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...
Protein Organization01:24

Protein Organization

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.
Protein Organization01:13

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Overview
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Updated: Jul 1, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Peptoid architectures: elaboration, actuation, and application.

Barney Yoo1, Kent Kirshenbaum

  • 1Department of Chemistry, New York University, 100 Washington Square E., Room 1001, New York, NY 10003, USA.

Current Opinion in Chemical Biology
|September 13, 2008
PubMed
Summary
This summary is machine-generated.

Peptoids, or N-substituted glycine oligomers, offer precise sequence control for creating diverse compound libraries. New methods now direct their backbone conformation, enabling the discovery of protein mimetics.

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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

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Last Updated: Jul 1, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

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

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Area of Science:

  • Polymer Chemistry
  • Biomolecular Engineering
  • Medicinal Chemistry

Background:

  • Peptoids are peptidomimetics built from N-substituted glycine units.
  • Their synthesis allows for precise control over monomer sequence and library generation.
  • Understanding peptoid sequence-structure-function relationships is an emerging research area.

Purpose of the Study:

  • To explore new methods for controlling peptoid backbone conformation.
  • To enable the formation of specific secondary structures in peptoids.
  • To advance the design and assembly of protein mimetics using peptoids.

Main Methods:

  • Development of novel synthetic strategies for peptoid backbone conformation control.
  • Investigation of methods to induce secondary structures like helices, loops, and turns.
  • Utilizing peptoid libraries to identify bioactive compounds.

Main Results:

  • Demonstrated successful direction of peptoid backbone conformation.
  • Achieved formation of defined secondary structures (helices, loops, turns).
  • Identified potential for discovering new bioactive peptoids.

Conclusions:

  • New approaches effectively control peptoid secondary structures.
  • These advances facilitate the discovery of bioactive peptoids.
  • Peptoids can serve as modules for designing protein mimetics.