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Antibiotic Selection

Antibiotic Selection

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Related Experiment Video

Updated: May 6, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Iterative antimicrobial candidate selection from informed d-/l-Peptide dimer libraries.

Roman J Lichtenecker¹, Bernhard Ellinger, Hong-Mei Han

¹Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany); Current address: Institute of Organic Chemistry, University of Vienna, Währingerstrasse 38, 1090 Wien (Austria).

Chembiochem : a European Journal of Chemical Biology

|October 24, 2013

Summary

This summary is machine-generated.

Researchers developed novel synthetic antimicrobial peptides (AMPs) by combining natural AMP sequences with a unique D-/L-stereochemistry backbone. These new peptide antibiotics show high efficacy against bacteria with low toxicity.

Keywords:

antibiotics compound libraries peptides screening solid-phase synthesis

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

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

Published on: January 26, 2016

Area of Science:

Medicinal Chemistry
Biotechnology
Microbiology

Background:

Antibiotic resistance and emerging pathogens necessitate novel therapeutic strategies.
Antimicrobial peptides (AMPs) show promise as alternative treatments.
Existing AMPs often face challenges with stability and production.

Purpose of the Study:

To design and synthesize a new class of synthetic antimicrobial peptides.
To explore a novel library design concept for AMP discovery.
To identify potent and safe peptide antibiotics against resistant bacteria.

Main Methods:

Stochastic distribution of natural AMP amino acid sequences onto synthetic peptides.
Incorporation of a D-/L-backbone stereochemistry motif for beta-helix formation.
Covalent recombination of permuted half-length sequences to create compound arrays.
Screening of synthetic peptides against Gram-positive and Gram-negative bacteria.
Optimization of lead compounds and characterization of mechanism of action via cryo-electron microscopy.

Main Results:

Identified and optimized synthetic D-/L-peptides with high antimicrobial activity.
Achieved broad-spectrum activity against both Gram-positive and Gram-negative bacteria.
Demonstrated low hemolytic activity, indicating reduced host toxicity.
Elucidated the membrane-associated mechanism of action using cryo-electron microscopy.

Conclusions:

The novel D-/L-peptide design strategy is effective for discovering potent antimicrobial agents.
These synthetic peptides represent a promising new class of antibiotics to combat bacterial infections.
Further development could lead to new therapeutic options against drug-resistant bacteria.