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Biotin-SARS-CoV-2 Spike RBD 523-541 peptide

Biotin-SARS-CoV-2 Spike RBD 523-541 peptide is the biotinylated version of SARS-CoV-2 Spike RBD 523-541 peptide. SARS-CoV-2 Spike RBD 523-541 peptide is an epitope of interest of the SARS-CoV-2 Spike S glycoprotein Receptor-Binding Domain (RBD). Biotin-SARS-CoV-2 Spike RBD 523-541 peptide is useful for vaccine development and for structure-activity relationship studies.

SARS-CoV-2 Spike (S) glycoprotein

Spike (S) glycoprotein corresponds to one of the leading targets for COVID-19 disease. Present on the surface of Sars-CoV-2 virus, Spike S protein is a class I fusion protein that allows the virus to enter host cells.

With a 1 273 aa length, Spike protein has 2 subunits : S1 contains the receptor-binding domain RBD and S2 induces the fusion of the viral envelop with the cellular membrane.

SARS-CoV-2 Spike RBD

The receptor-binding domain in SARS-CoV-2 Spike protein allows binding to the Angiotensin-Converting Enzyme receptor 2 (ACE2 receptor) which mediates the viral entry.



Technical specification

 Biotin-SARS-CoV-2 Spike RBD 523-541 buy Sequence : Biotin-TVCGPKKSTNLVKNKCVNF
 Biotin-SARS-CoV-2 Spike RBD 523-541 synthesis MW : 2306,77g/mol (C100H168N28O28S3)
 Biotin-SARS-CoV-2 Spike RBD 523-541 price Purity : > 95%
Peptide Library synthesis Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis Biotin-SARS-CoV-2 Spike RBD 523-541 Delivery format : Freeze dried in propylene 2mL microtubes
peptide solubility guidelines Peptide Solubility Guideline
buy peptide price Bulk peptide quantities available


Product catalog Size Price € HT Price $ HT
SB109-1MG 1 mg 156 195



1- Jun Lan et al. Nature. 581(7807):215-220 (2020)
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world1,2,3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses1,2,3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.

2- Wanbo Tai et al. Cell Mol Immunol. 17(6):613-620 (2020)
Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine

The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.