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Related Concept Videos

Stability of Substituted Cyclohexanes02:30

Stability of Substituted Cyclohexanes

12.3K
This lesson discusses the stability of substituted cyclohexanes with a focus on energies of various conformers and the effect of 1,3-diaxial interactions.
The two chair conformations of cyclohexanes undergo rapid interconversion at room temperature. Both forms have identical energies and stabilities, each comprising equal amounts of the equilibrium mixture. Replacing a hydrogen atom with a functional group makes the two conformations energetically non-equivalent.
For example, in...
12.3K
Conformations of Cyclohexane02:11

Conformations of Cyclohexane

12.1K
Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
12.1K
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

14.3K
The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
14.3K
Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.7K
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

432
In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
432
Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

324
In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
324

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Peptide-Bismuth Tricycles: Maximizing Stability by Constraint.

Lani J Davies1, Pritha Ghosh1, Sauhta Siryer1

  • 1Research School of Chemistry, Australian National University, Canberra, ACT, 2601, Australia.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 13, 2025
PubMed
Summary

Researchers developed a novel peptide-bismuth tricycle, enhancing drug discovery. This stable, potent protease inhibitor overcomes bioavailability challenges, showing promise for targeted therapies.

Keywords:
BismuthMacrocyclizationMulticyclesNanobodiesPeptides

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

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Related Experiment Videos

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Constrained peptides are valuable for drug discovery, but stability and bioavailability are major hurdles.
  • Genetically encoded libraries facilitate discovery of selective, high-affinity peptide ligands.
  • Overcoming peptide instability is crucial for therapeutic applications.

Purpose of the Study:

  • To develop a novel peptide constraint strategy using bismuth binding.
  • To evaluate the stability and inhibitory activity of bismuth-constrained peptides.
  • To explore the therapeutic potential of these enhanced peptide structures.

Main Methods:

  • Generated linear, cyclic, bicyclic, and tricyclic peptides with identical sequences using bismuth binding.
  • Compared different levels of peptide constraint by rigidifying structure with bismuth.
  • Assessed peptide stability in cellular glutathione and human plasma.
  • Evaluated protease inhibition activity and proteolytic resistance.
  • Conjugated a peptide-bismuth analogue to nanobodies via oxime ligation.

Main Results:

  • Identified a peptide-bismuth tricycle with exceptional stability against glutathione and human plasma degradation.
  • The tricycle demonstrated nanomolar protease inhibition and resistance to proteolytic digestion.
  • No non-canonical amino acid modifications were required for this enhanced stability and activity.
  • Demonstrated potential therapeutic applications by conjugating the tricycle to nanobodies.

Conclusions:

  • Bismuth-mediated macrocyclization is an effective strategy to enhance peptide stability and bioavailability.
  • The developed peptide-bismuth tricycle represents a promising lead compound for drug discovery.
  • This approach offers a versatile platform for developing peptide-based therapeutics with improved drug-like properties.