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Preparation of 1° Amines: Azide Synthesis01:22

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Direct alkylation of ammonia produces polyalkylated amines, along with a quaternary ammonium salt. To exclusively prepare primary amines, the azide synthesis method can be used.
Azide ions act as good nucleophiles and react with unhindered alkyl halides to form alkyl azides. Alkyl azides do not participate in further nucleophilic substitution reactions, thereby eliminating the chances of polyalkylated products. Alkyl azides are reduced by hydride-based reducing agents, like lithium aluminum...
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Aryldiazonium Salts to Azo Dyes: Diazo Coupling01:11

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The reaction of weakly electrophilic aryldiazonium (also called arenediazonium) salts with highly activated aromatic compounds leads to the formation of products with an —N=N— link, called an azo linkage. This reaction, presented in Figure 1, is known as diazo coupling and occurs without the loss of the nitrogen atoms of the aryldiazonium salt. Highly activated aromatic compounds such as phenols or arylamines favor the diazo coupling reaction. The coupling generally occurs at the para...
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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed

Veronica Diaz-Rodriguez1, Erh-Ting Hsu2, Elena Ganusova3

  • 1Department of Chemistry, University of Minnesota , 207 Pleasant Street SE, Minneapolis, Minnesota 55455, United States.

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Modified isoprenoids with azide and alkyne groups can be used for metabolic labeling of prenylated proteins. These functionalized isoprenoids yield biologically active and fully processed prenylated proteins, aiding disease model studies.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Post-Translational Modifications
  • Chemical Biology

Background:

  • Protein prenylation is a critical post-translational modification involving isoprenoid addition to proteins.
  • The a-factor peptide serves as a model for studying the three-step processing of prenylated proteins.
  • Bio-orthogonal isoprenoid analogs are emerging tools for studying prenylated protein function and disease.

Purpose of the Study:

  • To prepare and utilize prenylated a-factor analogs and precursor peptides.
  • To assess the biological activity of a-factor analogs with modified isoprenoids.
  • To evaluate the processing efficiency of precursor peptides by yeast proteases and methyltransferases.

Main Methods:

  • Synthesis of a-factor analogs with azide- and alkyne-functionalized isoprenoids.
  • Preparation of a-factor-derived precursor peptides.
  • Enzymatic processing assays using yeast proteases (Rce1, Ste24) and methyltransferase (Ste14).

Main Results:

  • Modified isoprenoids did not interfere with the biological activity of a-factor analogs.
  • Precursor peptides were efficiently processed by yeast enzymes to yield mature a-factor analogs.
  • Metabolic labeling with functionalized isoprenoids produced fully processed and biologically functional prenylated products.

Conclusions:

  • Bio-orthogonal isoprenoids can be effectively used for metabolic labeling of prenylated proteins.
  • These modified isoprenoids yield functional and fully processed prenylated products.
  • The approach minimizes concerns about undesired physiological changes complicating data interpretation in disease models.