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Related Concept Videos

From DNA to Protein03:06

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
The Central Dogma01:25

The Central Dogma

Overview
The Central Dogma01:20

The Central Dogma

The central dogma explains the flow of genetic information from DNA nucleotides to the amino acid sequence of proteins.
RNA is the Missing Link Between DNA and Proteins
In the early 1900s, scientists discovered that DNA stores all the information needed for cellular functions and that proteins perform most of these functions. However, the mechanisms of converting genetic information into functional proteins remained unknown for many years. Initially, it was believed that a single gene is...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

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Updated: Jun 18, 2026

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

Diverse backbone-cyclized peptides via codon reprogramming.

Takashi Kawakami1, Atsushi Ohta, Masaki Ohuchi

  • 1Department of Chemistry and Biotechnology, The University of Tokyo, Japan.

Nature Chemical Biology
|November 17, 2009
PubMed
Summary

This study introduces a novel ribosomal synthesis method for backbone-cyclized peptides using genetic code reprogramming. The technique enables the creation of complex cyclic peptides, including naturally occurring and novel bioactive sequences.

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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Peptide Chemistry

Background:

  • Backbone-cyclized peptides are a significant class of natural products with diverse biological activities.
  • Current methods for synthesizing these complex molecules are often challenging and limited in scope.
  • Genetic code reprogramming offers a powerful tool for introducing non-canonical amino acids into peptides.

Purpose of the Study:

  • To develop a novel, efficient methodology for the ribosomal synthesis of backbone-cyclized peptides.
  • To utilize genetic code reprogramming for the site-specific incorporation of nonproteinogenic amino acids.
  • To demonstrate the versatility of the method by synthesizing naturally occurring and novel cyclic peptides.

Main Methods:

  • Genetic code reprogramming to introduce nonproteinogenic amino acids.
  • Ribosomal expression of linear peptides containing a cysteine-proline dipeptide sequence.
  • Chemical treatment with glycolic acid to induce self-rearrangement to a diketopiperadine-thioester.
  • Non-enzymatic generation of the final cyclized peptide.

Main Results:

  • Successful ribosomal synthesis of backbone-cyclized peptides.
  • Demonstration of the method using naturally occurring cyclic peptides.
  • Creation of a library of peptides based on a bicyclic scaffold.
  • Identification of bioactive sequences through screening and deconvolution.

Conclusions:

  • The developed methodology provides a robust platform for the synthesis of diverse backbone-cyclized peptides.
  • This approach expands the accessible chemical space for cyclic peptide discovery.
  • The method facilitates the identification of novel bioactive cyclic peptides with potential therapeutic applications.