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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.
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Related Experiment Video

Updated: Jun 2, 2026

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

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Published on: August 1, 2018

Peptide Drug Discovery through Secondary Structure Control.

Yosuke Demizu^1,2,3

¹Division of Organic Chemistry, National Institute of Health Sciences.

Chemical & Pharmaceutical Bulletin

|May 31, 2026

Summary

This summary is machine-generated.

Controlling peptide structure advances drug discovery. Stabilized alpha-helices enable new therapeutics for protein-protein interaction inhibition, antimicrobial functions, and drug delivery, with regulatory guidelines established.

Keywords:

antimicrobial peptide cell-penetrating peptide peptide drug discovery protein–protein interaction inhibition regulatory science secondary structure control

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Last Updated: Jun 2, 2026

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Area of Science:

Medicinal Chemistry
Biotechnology
Drug Discovery

Background:

Peptides offer therapeutic potential but face challenges due to conformational flexibility and poor drug-like properties.
Recent advances allow precise control over peptide secondary structures, transforming them into versatile design platforms.

Purpose of the Study:

To review research on peptide drug discovery using secondary structure control as a core design principle.
To demonstrate how modulating alpha-helical conformations regulates molecular recognition, membrane interactions, and cellular uptake.

Main Methods:

Rational modulation of alpha-helical conformations in peptide design.
Development of peptides targeting protein-protein interactions (PPIs).
Engineering of antimicrobial peptides and cell-penetrating peptides for drug delivery.

Main Results:

Successfully designed alpha-helix-based peptides for PPI inhibition.
Developed antimicrobial peptides with enhanced efficacy and reduced cytotoxicity.
Optimized cell-penetrating peptides for efficient nucleic acid delivery.
Extended stabilized helical peptides for targeted protein degradation applications.

Conclusions:

Secondary structure control is a fundamental strategy for next-generation peptide therapeutics.
This approach enables systematic regulation of peptide functions, expanding their therapeutic scope.
Translation of these findings into clinical practice is supported by established regulatory guidelines for peptide drugs.