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Related Concept Videos

Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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.
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
Protein Modifications in the RER01:26

Protein Modifications in the RER

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.
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

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Related Experiment Video

Updated: Jun 2, 2026

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry
10:18

Making Conjugation-induced Fluorescent PEGylated Virus-like Particles by Dibromomaleimide-disulfide Chemistry

Published on: May 27, 2018

Efficient disulfide bond formation in virus-like particles.

Bradley C Bundy1, James R Swartz

  • 1Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, United States. bundy@byu.edu

Journal of Biotechnology
|May 4, 2011
PubMed
Summary
This summary is machine-generated.

Researchers controlled disulfide bond formation in virus-like particles (VLPs) using redox potential in cell-free synthesis. This advancement enhances VLP applications in medicine and materials science.

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Area of Science:

  • Biotechnology
  • Nanotechnology
  • Structural Biology

Background:

  • Virus-like particles (VLPs) are non-infectious nano-capsules mimicking viral structures.
  • VLPs possess defined morphology, symmetry, and cargo encapsulation capabilities.
  • Current applications include vaccination, drug/gene delivery, imaging, sensing, and materials science.

Purpose of the Study:

  • To demonstrate control over disulfide bond formation in VLPs.
  • To investigate the influence of redox potential on VLP assembly and structure.
  • To optimize VLP production using open cell-free protein synthesis.

Main Methods:

  • Utilized open cell-free protein synthesis for VLP production.
  • Controlled redox potential during and after VLP production and assembly.
  • Analyzed disulfide bond formation under varying conditions.

Main Results:

  • Successfully controlled disulfide bond formation by manipulating redox potential.
  • Identified VLP-dependent optimal conditions for disulfide bond formation.
  • Observed a cooperative effect in the formation of disulfide bonds within VLPs.

Conclusions:

  • Redox potential is a key factor in controlling VLP structure and function.
  • Open cell-free synthesis provides a viable platform for VLP engineering.
  • Controlled disulfide bonds can enhance VLP utility in diverse applications.