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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 sequences.

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Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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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Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones

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Acetals are formed by reacting two equivalents of alcohol with carbonyl compounds like aldehydes or ketones. Acetals are unaffected by bases, nucleophiles, oxidizing agents, and reducing agents. They serve as protecting groups for aldehydes and ketones. Acetals can be easily formed and also easily removed via mild acid hydrolysis.
In the presence of multiple functional groups, when selective reduction of one group over the other is desired, groups like aldehydes and ketones that form acetals...

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Related Experiment Video

Updated: May 9, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Tunable thioesters as "reduction" responsive functionality for traceless reversible protein PEGylation.

Jianwei Chen¹, Mingkun Zhao, Fude Feng

¹Department of Pharmacology, Dan L. Duncan Cancer Center, and Cardiovascular Research Institute, Baylor College of Medicine, Houston, Texas 77030, USA.

Journal of the American Chemical Society

|July 16, 2013

Summary

Thioester chemistry offers a novel, tunable alternative to disulfide bonds for reduction-responsive drug delivery. This thiol-responsive system is easier to synthesize and provides broader kinetic control than traditional methods.

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Published on: June 21, 2021

Area of Science:

Chemical Biology
Drug Delivery Systems
Materials Science

Background:

Disulfide bonds are the primary reduction-responsive triggers used in current drug delivery technologies.
Existing disulfide-based systems have limitations in synthetic accessibility and kinetic tunability.

Purpose of the Study:

To introduce and characterize thioester as a novel thiol-responsive chemistry for advanced drug delivery applications.
To explore the tunable reactivity of thioesters by modifying their steric environment.
To develop a traceless, reversible protein PEGylation reagent utilizing thioester chemistry.

Main Methods:

Synthesis and characterization of thioester compounds with varying steric environments.
Kinetic studies to evaluate the reactivity and tunability of thioester linkages.
Development and testing of a novel protein PEGylation reagent based on thioester chemistry.

Main Results:

Thioesters demonstrate facile synthesis and an order of magnitude broader kinetic tunability compared to disulfides.
Reactivity of thioesters can be precisely modulated by adjusting the steric bulk around the thioester linkage.
A novel traceless and reversible protein PEGylation reagent was successfully developed using thioester chemistry.

Conclusions:

Thioester chemistry represents a versatile and highly tunable platform for developing next-generation reduction-responsive drug delivery systems.
The facile synthesis and broad kinetic control offered by thioesters overcome limitations of current disulfide-based approaches.
The developed thioester-based PEGylation reagent shows promise for advanced bioconjugation strategies.