Selected article for: "amino acid and high density"
Author: So Young Kim; Weihua Jin; Amika Sood; David W. Montgomery; Oliver C. Grant; Mark M. Fuster; Li Fu; Jonathan S. Dordick; Robert J. Woods; Fuming Zhang; Robert J. Linhardt
Title: Glycosaminoglycan binding motif at S1/S2 proteolytic cleavage site on spike glycoprotein may facilitate novel coronavirus (SARS-CoV-2) host cell entry
  • Document date: 2020_4_15
    • ID: fs8dn7ir_9
    Snippet: The extremely high binding affinity of SARS-CoV-2 SGP to HP was supported by the chip surface regeneration conditions. The immobilized HP surface could only be regenerated using a harsh regeneration reagent, 0.25% SDS, instead of the standard 2M NaCl solution used for removing HP-binding proteins. One reason for SARS-CoV-2 SGP monomer and trimer extremely high affinity to immobilized heparin is the high density of surface bound ligands might prom.....
    Document: The extremely high binding affinity of SARS-CoV-2 SGP to HP was supported by the chip surface regeneration conditions. The immobilized HP surface could only be regenerated using a harsh regeneration reagent, 0.25% SDS, instead of the standard 2M NaCl solution used for removing HP-binding proteins. One reason for SARS-CoV-2 SGP monomer and trimer extremely high affinity to immobilized heparin is the high density of surface bound ligands might promote polyvalent interactions. The difference of binding kinetics and affinity of CoV SGPs to HP may also be due in part to the difference in protein sequence of the Cov SGPs. Based on amino acid alignment analysis using the Basic Local Alignment Search Tool (BLAST), SARS-CoV and SARS-CoV-2 SGPs share 76% similarity. Association rate constants (ka) for MERS-CoV SGP (339 (± 27) 1/M -1 s 1 ) was the lowest, followed by monomeric and trimeric SARS-CoV-2 SGP (2.5 author/funder. All rights reserved. No reuse allowed without permission.

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