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10.1016/j.compbiolchem.2022.107668 http://scihub22266oqcxt.onion/10.1016/j.compbiolchem.2022.107668 35339763!8941845!35339763     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Comput+Biol+Chem 2022 ; 98 (ä): 107668 Nephropedia Template TP {{tp|p=35339763|t=2022. Glycosylation is key for enhancing drug recognition into spike glycoprotein of SARS-CoV-2 |pdf=|usr=}}{{35339763}} gab.com Text Glycosylation is key for enhancing drug recognition into spike glycoprotein of SARS-CoV-2 JO: Comput Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=35339763 #FOAvip The emergence of COVID-19 caused by SARS-CoV-2 and its spread since 2019 represents the major public health problem worldwide nowadays, which has generated a high number of infections and deaths. The spike protein (S protein) is the most studied protein of SARS-CoV-2, and key to host-cell entry through ACE2 receptor. This protein presents a large pattern of glycosylations with important roles in immunity and infection mechanisms. Therefore, understanding key aspects of the molecular mechanisms of these structures, during drug recognition in SARS-CoV-2, may contribute to therapeutic alternatives. In this work, we explored the impact of glycosylations on the drug recognition on two domains of the S protein, the receptor-binding domain (RBD) and the N-terminal domain (NTD) through molecular dynamics simulations and computational biophysics analysis. Our results show that glycosylations in the S protein induce structural stability and changes in rigidity/flexibility related to the number of glycosylations in the structure. These structural changes are important for its biological activity as well as the correct interaction of ligands in the RBD and NTD regions. Additionally, we evidenced a roto-translation phenomenon in the interaction of the ligand with RBD in the absence of glycosylation, which disappears due to the influence of glycosylation and the convergence of metastable states in RBM. Similarly, glycosylations in NTD promote an induced fit phenomenon, which is not observed in the absence of glycosylations; this process is decisive for the activity of the ligand at the cryptic site. Altogether, these results provide an explanation of glycosylation relevance in biophysical properties and drug recognition to S protein of SARS-CoV-2, which must be considered in the rational drug development and virtual screening targeting S protein. Twit Text FOAVip Glycosylation is key for enhancing drug recognition into spike glycoprotein of SARS-CoV-2 ????Comput Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=35339763 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35339763 #FOAvip English Wikipedia <ref>{{Cite pmid|35339763}}</ref> Glycosylation is key for enhancing drug recognition into spike glycoprotein of SARS-CoV-2 #MMPMID35339763 Ropon-Palacios G; Perez-Silva J; Rojas-Humpire R; Olivos-Ramirez GE; Chenet-Zuta M; Cornejo-Villanueva V; Carmen-Sifuentes S; Otazu K; Ramirez-Diaz YL; Chozo KV; Camps I Comput Biol Chem 2022[Jun]; 98 (ä): 107668 PMID35339763show ga The emergence of COVID-19 caused by SARS-CoV-2 and its spread since 2019 represents the major public health problem worldwide nowadays, which has generated a high number of infections and deaths. The spike protein (S protein) is the most studied protein of SARS-CoV-2, and key to host-cell entry through ACE2 receptor. This protein presents a large pattern of glycosylations with important roles in immunity and infection mechanisms. Therefore, understanding key aspects of the molecular mechanisms of these structures, during drug recognition in SARS-CoV-2, may contribute to therapeutic alternatives. In this work, we explored the impact of glycosylations on the drug recognition on two domains of the S protein, the receptor-binding domain (RBD) and the N-terminal domain (NTD) through molecular dynamics simulations and computational biophysics analysis. Our results show that glycosylations in the S protein induce structural stability and changes in rigidity/flexibility related to the number of glycosylations in the structure. These structural changes are important for its biological activity as well as the correct interaction of ligands in the RBD and NTD regions. Additionally, we evidenced a roto-translation phenomenon in the interaction of the ligand with RBD in the absence of glycosylation, which disappears due to the influence of glycosylation and the convergence of metastable states in RBM. Similarly, glycosylations in NTD promote an induced fit phenomenon, which is not observed in the absence of glycosylations; this process is decisive for the activity of the ligand at the cryptic site. Altogether, these results provide an explanation of glycosylation relevance in biophysical properties and drug recognition to S protein of SARS-CoV-2, which must be considered in the rational drug development and virtual screening targeting S protein. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Glycoproteins[MESH] |Glycosylation[MESH] |Humans[MESH] |Ligands[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH]Glycosylation is key for enhancing drug recognition into spike glycopr(epmc).pdf DeepDyve Pubget Overpricing