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Related Concept Videos

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 and Protein Structure02:15

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 can...
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene π orbitals.
Hybridization of Atomic Orbitals II03:35

Hybridization of Atomic Orbitals II

sp3d and sp3d 2 Hybridization
Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the involved orbitals. The...
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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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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"Bridged" n→π* interactions can stabilize peptoid helices.

Benjamin C Gorske1, Ryan C Nelson, Zara S Bowden

  • 1Department of Chemistry, Bowdoin College , 6600 College Station, Brunswick, Maine 04011-8466, United States.

The Journal of Organic Chemistry
|September 21, 2013
PubMed
Summary

Peptoids and thiopeptoids folding can be controlled by engineering specific side-chain interactions. This study reveals new strategies for stabilizing structures in these peptidomimetics for therapeutic applications.

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Area of Science:

  • Chemical Biology
  • Supramolecular Chemistry
  • Materials Science

Background:

  • Peptoids, a class of peptidomimetic foldamers, are valuable in diverse applications including therapeutics and catalysis.
  • Controlling peptoid secondary structures is crucial for their function, with side-chain engineering being a key strategy.
  • N→π*(Ar) interactions are important for stabilizing helical structures in aromatic peptoids.

Purpose of the Study:

  • To investigate n→π*(Ar) interactions in peptoid and thiopeptoid models.
  • To characterize a novel
  • bridged
  • interaction mode.
  • To explore strategies for controlling peptoid and thiopeptoid folding.

Main Methods:

  • Computational modeling of peptoid and thiopeptoid structures.
  • Experimental validation of predicted interactions.
  • Analysis of amide rotamerism and secondary structure stabilization.

Main Results:

  • N→π*(Ar) interactions significantly influence amide rotamerism in both peptoids and thiopeptoids.
  • A new "bridged" interaction mode involving N-α-C-H σ orbitals was characterized.
  • Thiopeptoids exhibit significant structural ordering due to these interactions.

Conclusions:

  • N→π*(Ar) interactions offer a powerful strategy for controlling peptoid and thiopeptoid folding.
  • Thiopeptoids show promise as highly structured molecules for therapeutic and nanotechnological applications.
  • This research provides new insights into the fundamental principles governing foldamer structure and function.