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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.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
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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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Bacterial Protein Maturation01:26

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Protein Glycosylation01:25

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Related Experiment Video

Updated: Sep 10, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Late-Stage Serine Modification Enables Noncanonical Peptide Synthesis.

Zhenyan Guo1, Tianning Diao1

  • 1Department of Chemistry, New York University, 100 Washington Square East, New York, New York 10003, United States.

Journal of the American Chemical Society
|August 25, 2025
PubMed
Summary

This study introduces a novel method for late-stage modification of serine residues in peptides. This approach enables the synthesis of diverse noncanonical amino acids, advancing peptide drug discovery.

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Area of Science:

  • Medicinal Chemistry
  • Organic Synthesis
  • Peptide Chemistry

Background:

  • Noncanonical amino acids enhance drug properties but are synthetically challenging to incorporate.
  • Late-stage modification of natural residues offers an efficient strategy for analogue library generation.
  • Existing deoxygenative methods are incompatible with complex peptides, limiting serine modification.

Purpose of the Study:

  • To develop a site-selective, late-stage deoxygenative functionalization method for serine residues in peptides.
  • To enable the transformation of serine into various noncanonical amino acid residues.
  • To provide a versatile platform for peptide diversification in medicinal chemistry.

Main Methods:

  • Utilized a phosphoramidite reagent and a photocatalytic system for serine deoxygenative activation.
  • Employed radical addition to diverse acceptors for functionalization.
  • Applied the method to complex peptides (enkephalin, bradykinin, α-MSH) on solid support and in solution.

Main Results:

  • Achieved site-selective, late-stage deoxygenative functionalization of serine residues.
  • Transformed serine into noncanonical residues like homoglutamine, homoglutamic acid, 5-hydroxynorvaline, phosphonates, and alanine-3-d1.
  • Demonstrated compatibility with complex peptides, showcasing broad substrate scope and robustness.

Conclusions:

  • Developed a novel, versatile method for late-stage serine modification in peptides.
  • Enabled efficient generation of diverse noncanonical amino acid-containing peptides.
  • Advanced peptide diversification strategies for medicinal chemistry applications.