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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

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Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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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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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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Related Experiment Video

Updated: May 13, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Sulfur(IV) Chemistry-Based Peptide and Protein Late-Stage Modification.

Dongyan Yang1, Zhijun Ruan2, Shiliang He3

  • 1College of Chemistry and Chemical Engineering, Zhongkai University of Agriculture and Engineering, Guangzhou, 510230, China.

Chembiochem : a European Journal of Chemical Biology
|April 16, 2025
PubMed
Summary
This summary is machine-generated.

New sulfur(IV) chemistry enables precise peptide and protein modification, overcoming limitations of current methods. This advance offers new tools for studying biological functions and developing advanced macromolecular therapeutics.

Keywords:
late‐stage modificationpeptideproteinsulfiliminesulfoniumsulfur(IV) chemistry

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Area of Science:

  • Chemical Biology
  • Biochemistry
  • Medicinal Chemistry

Background:

  • Precise chemical modification of peptides and proteins is crucial for understanding structure-activity relationships and developing therapeutics.
  • Existing methods like irreversible covalent labeling and unnatural amino acid incorporation have limitations in reversibility, in situ regulation, and physiological adaptability.

Purpose of the Study:

  • To review recent advancements in sulfur(IV) chemistry for peptide and protein modification.
  • To highlight the potential of these new strategies for various applications, including proximity labeling and drug delivery.

Main Methods:

  • Synergistic innovations in sulfur(IV)-based reagent design.
  • Modulation of reaction intermediates.
  • Development of bioorthogonal reactions for site-selective modification.

Main Results:

  • Establishment of a versatile modification toolbox with site selectivity, condition responsiveness, and functional rescue capabilities.
  • Demonstration of sulfur(IV) chemistry as a powerful platform for late-stage functionalization of biomolecules.

Conclusions:

  • Sulfur(IV) chemistry offers a promising alternative to existing methods for peptide and protein modification.
  • These advancements hold significant potential for future applications in chemical biology and therapeutic interventions.