Cysteine-based VLP-Peptide Conjugation Service

Cysteine-based VLP-Peptide Conjugation Service

As the world's leading customized service provider, CD BioSciences has a sophisticated VLPlant^TM platform , advanced equipment and experienced scientists, dedicated to helping our customers connect peptides and VLPs through cysteine-based modification. Working closely with our customers and experts, we are happy to meet each of our specific requirements in order to provide the optimal solution.

VLP-Peptide Conjugation

The stoichiometry of peptide display is defined by the quaternary structure, and the self-assembly of the capsid in vivo requires less processing and a more homogeneous final product. Peptides can be linked to VLPs by genetic fusion or chemical conjugation methods, developing cVLPs. The chemical conjugation methods include cysteine modification, lysine modification, acidic amino acid modification and the like.

Cysteine-based VLPs Modifications

Cysteine is the most commonly used reactive amino acid residue that can be presented on the surface of VLPs by natural presentation or mutation. However, disulfide bonds can also be easily reduced if the ligand is not an ideal surface attachment for VLPs. At pH values between 6.5 and 7.5, a range of compounds based on maleimide are able to form irreversible thioether attachments to cysteine residues. This attachment method has been widely used to attach fluorescent probes, peptides and proteins to the surface of VLPs.

Cysteine-based VLPs modifications. (Chen CC, et al., 2018)

Cysteine-based VLP-Peptide Conjugation

The most common protein PTM regulation method is phosphorylation/dephosphorylation, in addition to a unique PTM method, the multifunctional redox modification of cysteine residues. Although cysteine does not occupy a high proportion in the amino acid sequence of proteins, it is widely used in the selective modification of proteins due to its remarkable nucleophilicity, redox properties and easy modification properties.

Among them, the Michael addition reaction of maleimide and vinyl sulfone with sulfhydryl is a very classic sulfhydryl modification reaction, and it is a better method for modifying cysteine in proteins. Cysteine is the most commonly used reactive amino acid residue and can be presented on the surface of VLPs either by natural presentation or by mutation. When the pH was between 6.5 and 7.5, VLPs and peptides were activated using maleimide, which were then irreversibly bound by thioether bonds under the action of the heterojunction.

Our Services

CD BioSciences has a sophisticated VLPlant^TM platform and extensive experience in providing cysteine-based VLP-peptide conjugation. We have the ability and confidence to meet your needs for rapid and accurate development of cVLPs. Of course, you can also contact us directly, we are happy to hear from you and look forward to working with you.

The Workflow of Cysteine-based VLP-Peptide Conjugation

Why Choose CD BioSciences

Experienced
We provide global customers with services of linking peptides and VLPs based on cysteine modification for a long time and are good at solving difficulties and challenges encountered in the experimental process.

Flexible
We maintain close contact with customers, discuss problems encountered in the experimental process in a timely manner, and meet your specific requirements.

High Quality
We have the ability and confidence to provide you with the best experimental solution to meet your needs for fast and accurate linking of peptides to VLPs.

Reference

1. Chen CC.; et al. Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods. J Vis Exp. 2018,135:1-8.