In the second study, based on the detected correlations in the covariance matrix between pairs of residues, the authors confirmed the stability of the vaccine candidate model. Rafi et al. performed classical MD simulations to check the stability of the constructed vaccine with the extracellular subunit of TLR2 and TLR4/MD2. The results indicated that the TLR-vaccine complexes were both stable and compact during the simulations. Especially for the TLR4vaccine complex, a strong hydrogen bond network was pointed out, suggesting reduced flexibility of the vaccine when bound to the receptor, improved binding strength, and increased vaccine-receptor stability. Furthermore, the authors expanded their analysis by using the fulllength heterodimer TLR4/MD2-vaccine complex which was placed in a membrane to imitate the dynamic behaviour during the MD simulation of the vaccine in biological systems. This study is one of the first where the full-length models of TLR receptors from the AlphaFold Protein Structure Database were used. For both TLR2 and TLR4 complexes, significant structural transitions toward membrane bilayer were observed, but the crucial interactions between the vaccine and the extracellular domain of receptors remained stable. Based on the observations made in the above-mentioned papers, one can speculate that during the binding, potentially welldesigned vaccines may have a stabilising effect on the TLRs in the system.