The<unk>  is a peptide. Consequently, it is a molecule formed by a sequence of amino-acids united by peptide bonds. If we compare both primary structures, it can be seen that the<unk>  has 2 subunits. Each subunit, monomer is a variant form, a mutant of the<unk> IP, differing from four amino acids. Thus, among the new ones introduced, it is important to emphasize the importance of the cysteine (C) introduced replacing the methionine (M),both being sulfated amino acids, in the stabilization of its structure.<unk>  can establish more hydrogen bonds because it has 41 H-bond donors and 56 H-bond acceptors in comparison with the 23 H-bond donors and 30 H-bond acceptors of the<unk> IP.Therefore, it's able to form more interactions and react with the gp-41 in a higher intensity than the<unk> IP. Another important interaction that we must underline is the disulfide bond established between both cysteines of the two monomers of the<unk>  which allows the peptide to have more structural stability in the space in comparison with the<unk> IP. Moreover, the ring form that appears in the secondary structure is due to this interaction between both sulfate atoms. Thanks to this disulfide bond, a cystine is formed. This fact allows the union of the subunits during the reaction with the gp41 and also allows them to act simultaneously. Thanks to all this activity and to the dimerization respect to the<unk> IP, the<unk>  is more effective.
VIR-576
BGR-34
NFPA 704
GRAd-COV2
C-KAD
COVAX-19
SRD5A3-CDG
CURB-65