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

Diels–Alder Reaction Forming Bridged Bicyclic Products: Stereochemistry01:29

Diels–Alder Reaction Forming Bridged Bicyclic Products: Stereochemistry

Diels–Alder reactions between cyclic dienes locked in an s-cis configuration and dienophiles yield bridged bicyclic products.
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

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 staggered...
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...
Conformations of Cyclohexane02:11

Conformations of Cyclohexane

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 tetrahedral value,...
Polymer Classification: Stereospecificity01:26

Polymer Classification: Stereospecificity

Polymerization generates chiral centers along the entire backbone of a polymer chain. Accordingly, the stereochemistry of the substituent group has a significant effect on polymer properties. Polymers formed from monosubstituted alkene monomers feature chiral carbons at every alternate position in the polymer backbone. Relative to the predominant orientation of substituents at the adjacent chiral carbons, the polymer can exist in three different configurations: isotactic, syndiotactic, and...
Stereoisomerism of Cyclic Compounds02:33

Stereoisomerism of Cyclic Compounds

In this lesson, we delve into the role of ring conformation and its stability, which determines the spatial arrangement and, consequently, the molecular symmetry and stereoisomerism of cyclic compounds. 1,2-Dimethylcyclohexane is used as a case study to evaluate the possible number of stereoisomers. Here, given the multiple (n = 2) chiral centers, there are 2n = 4 possible configurations that lack a plane of symmetry, as the ring skeleton exists in a non-planar chair conformation. In addition,...

You might also read

Related Articles

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

Sort by
Same author

Generation of membrane-permeable cyclic peptides inhibiting protein-protein interaction.

Nature chemical biology·2026
Same author

RPA hyperphosphorylation hinders the resolution of R-loops and G-quadruplex-associated R-loops during RAS-driven senescence.

Nucleic acids research·2026
Same author

Yeast Display Technology Enables Rapid Discovery of Low-Nanomolar Macrocyclic Peptide Inhibitors of Human Angiotensin-Converting Enzyme 2.

Journal of medicinal chemistry·2026
Same author

Defining the reference proteomes for small extracellular vesicles and non-vesicular components.

Nature cell biology·2026
Same author

Proteome-Wide Multipoint Internal Calibration Curves for Evaluating Peptide-Level Linearity in Relative Quantitative Proteomics.

Journal of proteome research·2025
Same author

[Astragaloside IV alleviates D-GAL-induced endothelial cell senescence by promoting mitochondrial autophagy <i>via</i> inhibiting the PINK1/Parkin pathway].

Nan fang yi ke da xue xue bao = Journal of Southern Medical University·2025

Related Experiment Video

Updated: May 23, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Structurally diverse cyclisation linkers impose different backbone conformations in bicyclic peptides.

Shiyu Chen1, Julia Morales-Sanfrutos, Alessandro Angelini

  • 1Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.

Chembiochem : a European Journal of Chemical Biology
|April 12, 2012
PubMed
Summary

New linkers for creating bicyclic peptides were developed. These linkers significantly alter peptide conformation and function, offering a new way to generate diverse peptide macrocycle libraries for drug discovery.

More Related Videos

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Related Experiment Videos

Last Updated: May 23, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Area of Science:

  • Chemical Biology
  • Medicinal Chemistry
  • Structural Biology

Background:

  • Combinatorial libraries of structurally diverse peptide macrocycles are valuable for developing high-affinity ligands.
  • Understanding how linker modifications affect peptide conformation is crucial for ligand design.

Purpose of the Study:

  • To develop novel linkers for generating genetically encoded bicyclic peptides.
  • To investigate the impact of these new linkers on peptide backbone conformations and inhibitory activity.

Main Methods:

  • Development of two new cyclisation reagents with three thiol-reactive groups.
  • Cyclisation of linear peptides containing three cysteine residues.
  • Assessing inhibitory activity of modified bicyclic peptides against plasma kallikrein using K(i) measurements.
  • Structural analysis using solution-state Nuclear Magnetic Resonance (NMR) to identify NOE constraints.

Main Results:

  • The new linkers efficiently and selectively cyclised linear peptides.
  • Replacing the original mesitylene linker in PK15 with new linkers reduced inhibitory activity against plasma kallikrein by over 1000-fold.
  • Solution-state NMR revealed distinct NOE constraints in peptides formed with the new linkers, indicating significant conformational changes.
  • Linkers at the core of bicyclic peptide structures were shown to profoundly influence peptide conformation.

Conclusions:

  • Linkers play a critical structural role in peptide macrocycles.
  • Employing diverse cyclisation linkers in a combinatorial approach can generate topologically varied macrocycle libraries.
  • This strategy offers a promising avenue for the discovery of novel peptide-based therapeutics.