Related Experiment Video
Updated: Jul 14, 2025
11:09
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
10.8K
Exploring a β-Amino Acid with a Seven-Membered Ring Constraint as a Foldamer Building Block for Nontraditional
Nuri Seo1, Hoyang Son1, Yonghan Kim1
1Department of Chemistry, Yonsei University, Seoul 03722, Republic of Korea.
Organic Letters
|October 6, 2023
Summary
cis-2-aminocycloheptanecarboxylic acid (ACHpC) enables novel helical structures in unnatural peptides, including the 11/9-helix and interconvertible 12/10-helices, expanding foldamer design possibilities.
Area of Science:
- Peptide chemistry
- Supramolecular chemistry
- Organic chemistry
Background:
- Foldamers are artificial molecules mimicking protein secondary structures.
- Cycloheptane derivatives offer unique conformational properties for peptide design.
Purpose of the Study:
- To investigate the potential of 2-aminocycloheptanecarboxylic acid (ACHpC) isomers as building blocks for helical foldamers.
- To characterize the secondary structures promoted by cis-ACHpC in unnatural peptides.
Main Methods:
- Synthesis and incorporation of trans- and cis-ACHpC into peptide backbones.
- Structural analysis of resulting peptides using techniques like NMR spectroscopy and X-ray crystallography (implied).
- Computational modeling to understand conformational dynamics.
Main Results:
- Trans-ACHpC exhibited limited folding propensity in unnatural peptides.
- Cis-ACHpC successfully promoted non-traditional helical structures: the 11/9-helix in α/β-peptides and the 12/10-helix in β-peptides.
- The 12/10-helices formed by cis-ACHpC displayed interconvertible handedness in solution, driven by cycloheptane ring pseudorotation.
Conclusions:
- Cis-ACHpC is a valuable building block for creating novel helical foldamers with unique structural features.
- The dynamic interconversion of helical handedness in cis-ACHpC-containing peptides offers new avenues for designing responsive biomaterials.
Related Concept Videos
01:22Protein Folding
118.3K
Overview
118.3K
01:13Protein Organization
138.3K
Overview
138.3K
02:15Protein and Protein Structure
79.7K
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...
A protein's shape is critical to its function. For example, an enzyme...
79.7K
01:09Multi-pass Transmembrane Proteins and β-barrels
5.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.3K
02:02Chair Conformation of Cyclohexane
14.7K
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...
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
14.7K
03:03Amyloid Fibrils
9.6K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.6K