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Related Concept Videos

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation08:48

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

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A simple and general method for the synthesis of cyclic peptides using microwave irradiation is outlined. This procedure enables the synthesis of backbone cyclic peptides with a collection of different conformations while retaining the side chains and the pharmacophoric moieties., and therefore, allows to screen for the bioactive...
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A Fluorogenic Peptide Cleavage Assay to Screen the Proteolytic Activity of Proteases02:42

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This video demonstrates an assay to screen for the proteolytic activity of proteases using fluorogenic peptides. The protease recognizes its cleavage site on the peptide, cleaving it and separating the quencher from the fluorophore, enabling its fluorescence emission. The fluorescence signal is detected and analyzed to check for the cleavage efficiency of different peptide...
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Oxidative Cleavage of Alkenes: Ozonolysis01:46

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In ozonolysis, ozone is used to cleave a carbon–carbon double bond to form aldehydes and ketones, or carboxylic acids, depending on the work-up.
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Alkynes to Carboxylic Acids: Oxidative Cleavage02:01

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Alkynes undergo oxidative cleavage in the presence of oxidizing reagents like potassium permanganate and ozone. The triple bond — one σ bond and two π bonds — is completely cleaved, and the alkyne is oxidized to carboxylic acids. When warm and basic aqueous potassium permanganate is used as an oxidizing agent, alkynes are first converted to carboxylate salts via an unstable α-diketone intermediate. Further, a mild acid treatment protonates the carboxylate anions...
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We present a fluorogenic peptide cleavage assay that allows a rapid screening of the proteolytic activity of proteases on peptides representing the cleavage site of viral fusion peptides. This method can also be used on any other amino acid motif within a protein sequence to test for the protease...
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Cleavage and Blastulation01:33

Cleavage and Blastulation

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After a large-single-celled zygote is produced via fertilization, the process of cleavage occurs while zygotes travel through the uterine tube. Cleavage is a mitotic cell division that does not result in growth. With each round of successive cell division, daughter cells get increasingly smaller.
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Related Experiment Video

Updated: Jan 20, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Published on: January 26, 2016

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Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.

Yao Ouyang1, Yue Yu1, Lingyang Zhu2

  • 1Department of Chemistry and Howard Hughes Medical Institute, 600 South Mathews Avenue, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.

Journal of the American Chemical Society
|January 19, 2026
PubMed
Summary
This summary is machine-generated.

Researchers characterized novel enzymes from Pseudomonas strains that modify peptides. These enzymes perform unique hydroxylation and backbone cleavage, expanding the diversity of bacterial RiPP biosynthesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are generated through complex enzymatic modifications.
  • Understanding the enzymes involved is key to expanding the known RiPP structural diversity.

Purpose of the Study:

  • To characterize novel enzymes from two Pseudomonas biosynthetic gene clusters (BGCs), pfl and pos.
  • To elucidate new catalytic transformations in RiPP biosynthesis.

Main Methods:

  • Enzyme characterization of α-ketoglutarate-dependent HEXXH enzymes (PflC, PosC) and a nitroreductase fusion enzyme.
  • Mutational analysis of enzyme substrates and motifs.
  • Investigating leader peptide influence on enzyme activity.

Main Results:

  • PflC and PosC hydroxylate consecutive glutamine residues and perform oxidative backbone cleavage, forming an amide terminus, triggered by a C-terminal ARMD motif.
  • The first position of the ARMD motif is critical for recognition and cleavage.
  • PflC exhibits proteolytic activity independent of the leader peptide, suggesting modulation of selectivity.
  • A unique nitroreductase fusion enzyme installs Z-dehydrophenylalanine and hydroxylates Asp residues.

Conclusions:

  • The characterized enzymes expand the known catalytic repertoire for RiPP biosynthesis.
  • This study increases the structural diversity accessible through bacterial RiPP pathways.
  • Enzyme-leader peptide interactions play a role in modulating RiPP modification selectivity.