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10.1016/j.bpj.2021.06.017 http://scihub22266oqcxt.onion/10.1016/j.bpj.2021.06.017 34214538!8241576!34214538     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2021 ; 120 (14): 2785-2792 Nephropedia Template TP {{tp|p=34214538|t=2021. Biophysical properties of the isolated spike protein binding helix of human ACE2 |pdf=|usr=}}{{34214538}} gab.com Text Biophysical properties of the isolated spike protein binding helix of human ACE2 JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=34214538 #FOAvip The entry of the severe acute respiratory syndrome coronavirus 2 virus in human cells is mediated by the binding of its surface spike protein to the human angiotensin-converting enzyme 2 (ACE2) receptor. A 23-residue long helical segment (SBP1) at the binding interface of human ACE2 interacts with viral spike protein and therefore has generated considerable interest as a recognition element for virus detection. Unfortunately, emerging reports indicate that the affinity of SBP1 to the receptor-binding domain of the spike protein is much lower than that of the ACE2 receptor itself. Here, we examine the biophysical properties of SBP1 to reveal factors leading to its low affinity for the spike protein. Whereas SBP1 shows good solubility (solubility > 0.8 mM), circular dichroism spectroscopy shows that it is mostly disordered with some antiparallel beta-sheet content and no helicity. The helicity is substantial (>20%) only upon adding high concentrations (>/=20% v/v) of 2,2,2-trifluoroethanol, a helix promoter. Fluorescence correlation spectroscopy and single-molecule photobleaching studies show that the peptide oligomerizes at concentrations >50 nM. We hypothesized that mutating the hydrophobic residues (F28, F32, and F40) of SBP1, which do not directly interact with the spike protein, to alanine would reduce peptide oligomerization without affecting its spike binding affinity. Whereas the mutant peptide (SBP1(mod)) shows substantially reduced oligomerization propensity, it does not show improved helicity. Our study shows that the failure of efforts, so far, to produce a short SBP1 mimic with a high affinity for the spike protein is not only due to the lack of helicity but is also due to the heretofore unrecognized problem of oligomerization. Twit Text FOAVip Biophysical properties of the isolated spike protein binding helix of human ACE2 ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=34214538 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34214538 #FOAvip English Wikipedia <ref>{{Cite pmid|34214538}}</ref> Biophysical properties of the isolated spike protein binding helix of human ACE2 #MMPMID34214538 Das A; Vishvakarma V; Dey A; Dey S; Gupta A; Das M; Vishwakarma KK; Roy DS; Yadav S; Kesarwani S; Venkatramani R; Maiti S Biophys J 2021[Jul]; 120 (14): 2785-2792 PMID34214538show ga The entry of the severe acute respiratory syndrome coronavirus 2 virus in human cells is mediated by the binding of its surface spike protein to the human angiotensin-converting enzyme 2 (ACE2) receptor. A 23-residue long helical segment (SBP1) at the binding interface of human ACE2 interacts with viral spike protein and therefore has generated considerable interest as a recognition element for virus detection. Unfortunately, emerging reports indicate that the affinity of SBP1 to the receptor-binding domain of the spike protein is much lower than that of the ACE2 receptor itself. Here, we examine the biophysical properties of SBP1 to reveal factors leading to its low affinity for the spike protein. Whereas SBP1 shows good solubility (solubility > 0.8 mM), circular dichroism spectroscopy shows that it is mostly disordered with some antiparallel beta-sheet content and no helicity. The helicity is substantial (>20%) only upon adding high concentrations (>/=20% v/v) of 2,2,2-trifluoroethanol, a helix promoter. Fluorescence correlation spectroscopy and single-molecule photobleaching studies show that the peptide oligomerizes at concentrations >50 nM. We hypothesized that mutating the hydrophobic residues (F28, F32, and F40) of SBP1, which do not directly interact with the spike protein, to alanine would reduce peptide oligomerization without affecting its spike binding affinity. Whereas the mutant peptide (SBP1(mod)) shows substantially reduced oligomerization propensity, it does not show improved helicity. Our study shows that the failure of efforts, so far, to produce a short SBP1 mimic with a high affinity for the spike protein is not only due to the lack of helicity but is also due to the heretofore unrecognized problem of oligomerization. |*COVID-19[MESH] |*Peptidyl-Dipeptidase A/genetics/metabolism[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Humans[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH]Biophysical properties of the isolated spike protein binding helix of (epmc).pdf DeepDyve Pubget Overpricing