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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...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Overview of Advanced Functional Groups

Overview of Advanced Functional Groups

Functional groups are groups of atoms with specific chemical properties that occur within organic molecules and are sometimes denoted as “R”. Functional groups can “functionalize” a compound by enabling it to adopt different physical and chemical properties.
Types of Advanced Functional Groups
The table below summarizes some of the major functional groups in organic chemistry.

Extraction: Advanced Methods

Extraction: Advanced Methods

Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is...

Structures of Solids

Structures of Solids

Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...

Structural Isomerism

Structural Isomerism

Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can...

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Related Experiment Video

Updated: Feb 4, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

Recent structural advances in constrained helical peptides.

Kornelia J Skowron¹, Thomas E Speltz¹, Terry W Moore^1,2

¹Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois.

Medicinal Research Reviews

|October 12, 2018

Summary

Researchers are developing new ways to stabilize alpha-helices using constrained peptides. These advances focus on novel helix-stabilizing technologies and diverse tethering strategies for bicyclic helical peptides.

Keywords:

alpha helix helical peptides peptide chemistry protein-protein interactions

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Published on: August 1, 2018

Area of Science:

Biochemistry and Medicinal Chemistry
Peptide Chemistry

Background:

Alpha-helices (α-helices) are fundamental protein structures prevalent throughout the proteome.
Developing mimics of α-helices is crucial, particularly for designing inhibitors of protein-protein interactions.
Constrained helical peptides offer enhanced conformational and proteolytic stability, and sometimes cell permeability.

Purpose of the Study:

To review recent advancements in technologies for stabilizing helical peptides.
To highlight new strategies for diversifying constraints and tethers in peptide design.
To explore combination strategies for creating novel bicyclic helical peptides.

Main Methods:

Review of recent literature on constrained peptide synthesis and design.
Analysis of various helix-stabilizing technologies, including lactam formation and hydrocarbon stapling.
Examination of emerging constraint and tether diversification approaches.

Main Results:

Identification of novel helix-stabilizing technologies beyond traditional methods.
Demonstration of diverse strategies for introducing constraints and tethers.
Exploration of synergistic effects in combined strategies leading to bicyclic structures.

Conclusions:

Significant progress has been made in developing advanced helix-stabilizing technologies for peptides.
Diversification of constraint and tethering strategies expands the toolkit for designing stable helical peptides.
Emerging bicyclic helical peptides hold promise for various applications, including therapeutic development.