Title | Chemoenzymatic Synthesis of SARS-CoV-2 Homogeneous O-Linked Glycopeptides for Exploring Their Inhibition Functions |
Author | |
Corresponding Author | Wu,Zhigang; He,Yunjiao; Kong,Yun |
Publication Years | 2022
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DOI | |
Source Title | |
ISSN | 2373-8227
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EISSN | 2373-8227
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Volume | 8Issue:10 |
Abstract | Harnessing highly conserved peptides derived from the receptor binding domain (RBD) of spike (S) protein to construct peptide-based inhibitors is one of the most effective strategies to fight against the ever-mutating coronavirus SARS-CoV-2. But how the O-glycosylation affects their inhibition abilities has not been intensively explored. Herein, an intrinsic O-glycosylated peptide P320-334 derived from RBD was screened and homogeneous O-linked glycopeptides containing Tn (GalNAcα1-O-Ser/Thr), T (Galβ1-3GalNAcα1-O-Ser/Thr), sialyl-Tn (sTn, Siaα2-6GalNAcα1-O-Ser/Thr), and sialyl-T (sT, Siaα2-3Galβ1-3GalNAcα1-O-Ser/Thr) structures were first synthesized via chemoenzymatic strategies. Compared with the unglycosylated peptide, the binding of sT-P320-334 to hACE2 was enhanced to 133% and the inhibition capacity against RBD-hACE2 binding of sTn- and sT-P320-334 was significantly increased up to 150-410%. Thus, our results suggest the sialic acid residue on the terminal of short O-glycan structures might strengthen the inhibition capacities of these peptide-based inhibitors, which might provide novel optimization directions for the inhibitor design. |
Keywords | |
URL | [Source Record] |
Indexed By | |
Language | English
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SUSTech Authorship | Corresponding
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Funding Project | Shandong Province Key Research and Develop Program["2019 GSF 107048","2020CXGC010601"]
; National Natural Science Foundation of China["31500648","31971213"]
; Guangdong Basic, Applied Basic Research Foundation[2019A1515010647]
; Open Projects Fund of Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University[2019CCG08]
; Shenzhen Science and Technology Program[KQTD20200909113758004]
; Hebei Provincial Department of Human Resources and Social Security Grants["C201812","E2018100010"]
; Foundation of Hebei Educational Committee[QN2019217]
; Natural Science Foundation of Hebei Province[H2021208001]
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WOS Research Area | Pharmacology & Pharmacy
; Infectious Diseases
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WOS Subject | Chemistry, Medicinal
; Infectious Diseases
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WOS Accession No | WOS:000859282900001
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Publisher | |
Scopus EID | 2-s2.0-85138766314
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Data Source | Scopus
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Citation statistics |
Cited Times [WOS]:2
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Document Type | Journal Article |
Identifier | http://kc.sustech.edu.cn/handle/2SGJ60CL/402752 |
Department | School of Medicine |
Affiliation | 1.National Glycoengineering Research Center,Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology,State Key Laboratory of Microbial Technology,Shandong University,Qingdao,266237,China 2.School of Medicine,Southern University of Science and Technology,Shenzhen,518055,China 3.School of Health and Life Sciences,University of Health and Rehabilitation Sciences,Qingdao,266071,China 4.College of Food and Biology,Hebei University of Science and Technology,Shijiazhuang,050018,China |
Corresponding Author Affilication | School of Medicine |
Recommended Citation GB/T 7714 |
Rong,Yongheng,Wang,Xingyun,Mao,Weian,et al. Chemoenzymatic Synthesis of SARS-CoV-2 Homogeneous O-Linked Glycopeptides for Exploring Their Inhibition Functions[J]. ACS Infectious Diseases,2022,8(10).
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APA |
Rong,Yongheng.,Wang,Xingyun.,Mao,Weian.,Yuan,Fang.,Chen,Min.,...&Kong,Yun.(2022).Chemoenzymatic Synthesis of SARS-CoV-2 Homogeneous O-Linked Glycopeptides for Exploring Their Inhibition Functions.ACS Infectious Diseases,8(10).
|
MLA |
Rong,Yongheng,et al."Chemoenzymatic Synthesis of SARS-CoV-2 Homogeneous O-Linked Glycopeptides for Exploring Their Inhibition Functions".ACS Infectious Diseases 8.10(2022).
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