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SARS-CoV-2 Membrane (M) protein

The Membrane Protein (M-protein), also called SARS-CoV-2 M (N), is a glycoprotein which interacts with Nucleocapsid protein for packaging of the viral genome.

Available peptide libraries

Some proteins of Sars-CoV-2 are identified as leading targets for COVID-19 therapies. sb-PEPTIDE offers specific peptide libraries of Coronavirus Membrane protein and custom synthesis of specific libraries.

Membrane protein – peptide library – Reference #SB050

Coronavirus Membrane is a glycoprotein of 222 aa length.  The library is made of 53 peptides with a length of 15 amino acids and an overlap of 11 amino acids (without post-translational modification)

Membrane protein – biotinylated peptide library – Reference #SB050-biotin

The above library is also available with N-ter biotin.

 Technical specifications

SARS-CoV-2 Membrane (M) protein buy Peptides length : 15 aa
SARS-CoV-2 Membrane (M) protein buy peptide library Offset number : 11 aa
SARS-CoV-2 Membrane (M) protein peptide library Amount : 0,5mg or 5*0,5mg (for each peptide)
SARS-CoV-2 Membrane (M) protein standard price Quality : Crude, 100% LC-MS
SARS-CoV-2 Membrane (M) protein standard synthesis Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis SARS-CoV-2 Membrane (M) protein Delivery format : Lyophilized or in solution, in 96-well plate or microtubes
COVID-19 peptide library buy Price : Ask for your quote
SARS-CoV-2 Membrane (M) protein standard solubility guidelines Peptide Solubility Guideline



1- Bianchi Martina et al. (2020)
Sars-CoV-2 Envelope and Membrane Proteins: Differences from Closely Related Proteins Linked to Cross-species Transmission?




The Coronavirus disease (COVID-19) is a new viral infection caused by severe acute respiratory coronavirus 2 (SARS-CoV-2) that was initially reported in city of Wuhan, China and afterwards spread globally. Genomic analyses revealed that SARS-CoV-2 is phylogenetically related to severe acute respiratory syndrome-like (SARS-like) Pangolin and Bat coronavirus specific isolates. In this study we focused on two proteins of Sars-CoV-2 surface: Envelope protein and Membrane protein. Sequences from Sars-CoV-2 isolates and other closely related virus were collected from the GenBank through TBlastN searches. The retrieved sequences were multiply aligned with MAFFT. The Envelope protein is identical to the counterparts from Pangolin CoV MP798 isolate and Bat CoV isolates CoVZXC21, CoVZC45 and RaTG13. However, a substitution at position 69 where an Arg replace for Glu, and a deletion in position 70 corresponding to Gly or Cys in other Envelope proteins were found. The Membrane glycoprotein appears more variable with respect to the SARS CoV proteins than the Envelope: a heterogeneity at the N-terminal position, exposed to the virus surface, was found between Pangolin CoV MP798 isolate and Bat CoV isolates CoVZXC21, CoVZC45 and RaTG13. Mutations observed on Envelope protein are drastic and may have significant implications for conformational properties and possibly for protein-protein interactions. Mutations on Membrane protein may also be relevant because this protein cooperates with the Spike during the cell attachment and entry. Therefore, these mutations may influence interaction with host cells. The mutations that have been detected in these comparative studies may reflect functional peculiarities of the Sars-CoV-2 virus and may help explaining the epizootic origin the COVID-19 epidemic.

2- Thomas, S. Preprints (2020)
The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter semiSWEET



Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M), envelope protein (E), nucleocapsid protein (N) and the spike protein (S). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. The advantage and role of sugar transporter like structures in viruses are unknown. If they are involved in energy metabolism, they may aid in the rapid proliferation and replication of the virus. Biological experiments should be performed to validate the presence and function of the semiSWEET sugar transporter.

3- Lee YN et al. J Virol Methods (2005)
Thermal aggregation of SARS-CoV membrane protein



SARS-CoV membrane protein could be detected easily using Western blotting in non-denaturing condition but not regular denaturing treatment. Boiling treatment, causing the aggregation of SARS-CoV membrane protein in the stacking gels, results in the failure to detect the membrane protein in the separating gels. Aggregated membrane proteins could not be dissociated by 1% Triton-X 100, 6 M urea, or 2% SDS. The region with amino acid residues from 51 to 170 is responsible for thermal aggregation of SARS-CoV membrane protein. Hydrophobic regions with amino acid residues from 61 to 90, from 91 to 100, from 136 to 170, are essential for this protein aggregation. Thermal aggregation of SARS-CoV membrane protein is not unique among structural proteins of coronaviruses. However, SARS-CoV membrane protein seems to be more sensitive to heat treatment, since the membrane protein of MHV-JHM, another member of the Coronaviridae, would not aggregate after the same treatment. Therefore, if SARS-CoV membrane protein needs to be analyzed using SDS-PAGE, boiling should be avoided. Thermal aggregation of SARS-CoV membrane protein may be one of the reasons for the inactivation of this virus by heat. The unusual property of SARS-CoV membrane protein aggregation induced by heat also provides a model for the study of protein aggregation.