Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain
The present investigation focuses on the analysis of the interactions among human lactoferrin (LF), SARS-CoV-2 receptor-binding domain (RBD) and human angiotensin-converting enzyme 2 (ACE2) receptor in order to assess possible mutual interactions that could provide a molecular basis of the reported...
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| Veröffentlicht in: | International journal of molecular sciences 2022-05, Vol.23 (10), p.5436 |
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| container_title | International journal of molecular sciences |
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| creator | Piacentini, Roberta Centi, Laura Miotto, Mattia Milanetti, Edoardo Di Rienzo, Lorenzo Pitea, Martina Piazza, Paolo Ruocco, Giancarlo Boffi, Alberto Parisi, Giacomo |
| description | The present investigation focuses on the analysis of the interactions among human lactoferrin (LF), SARS-CoV-2 receptor-binding domain (RBD) and human angiotensin-converting enzyme 2 (ACE2) receptor in order to assess possible mutual interactions that could provide a molecular basis of the reported preventative effect of lactoferrin against CoV-2 infection. In particular, kinetic and thermodynamic parameters for the pairwise interactions among the three proteins were measured via two independent techniques, biolayer interferometry and latex nanoparticle-enhanced turbidimetry. The results obtained clearly indicate that LF is able to bind the ACE2 receptor ectodomain with significantly high affinity, whereas no binding to the RBD was observed up to the maximum "physiological" lactoferrin concentration range. Lactoferrin, above 1 µM concentration, thus appears to directly interfere with RBD-ACE2 binding, bringing about a measurable, up to 300-fold increase of the K
value relative to RBD-ACE2 complex formation. |
| doi_str_mv | 10.3390/ijms23105436 |
| format | Article |
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value relative to RBD-ACE2 complex formation.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms23105436</identifier><identifier>PMID: 35628247</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>ACE2 ; Angiotensin ; Angiotensin-converting enzyme 2 ; Binding ; Binding sites ; Biosensors ; Complex formation ; Coronaviruses ; COVID-19 ; Domains ; Glycoproteins ; Interferometry ; Investigations ; Lactoferrin ; Latex ; Nanoparticles ; Peptidyl-dipeptidase A ; Proteins ; Severe acute respiratory syndrome coronavirus 2 ; Viruses</subject><ispartof>International journal of molecular sciences, 2022-05, Vol.23 (10), p.5436</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-f3caa757f2e3e8a0b31f4309df947856e30f06e0820b0d59acc12e5f90ef442f3</citedby><cites>FETCH-LOGICAL-c412t-f3caa757f2e3e8a0b31f4309df947856e30f06e0820b0d59acc12e5f90ef442f3</cites><orcidid>0000-0002-2762-9533 ; 0000-0003-1381-9560 ; 0000-0002-8253-940X ; 0000-0002-0043-8921 ; 0000-0002-3982-4141 ; 0000-0002-3064-0928</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141661/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141661/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35628247$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Piacentini, Roberta</creatorcontrib><creatorcontrib>Centi, Laura</creatorcontrib><creatorcontrib>Miotto, Mattia</creatorcontrib><creatorcontrib>Milanetti, Edoardo</creatorcontrib><creatorcontrib>Di Rienzo, Lorenzo</creatorcontrib><creatorcontrib>Pitea, Martina</creatorcontrib><creatorcontrib>Piazza, Paolo</creatorcontrib><creatorcontrib>Ruocco, Giancarlo</creatorcontrib><creatorcontrib>Boffi, Alberto</creatorcontrib><creatorcontrib>Parisi, Giacomo</creatorcontrib><title>Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>The present investigation focuses on the analysis of the interactions among human lactoferrin (LF), SARS-CoV-2 receptor-binding domain (RBD) and human angiotensin-converting enzyme 2 (ACE2) receptor in order to assess possible mutual interactions that could provide a molecular basis of the reported preventative effect of lactoferrin against CoV-2 infection. In particular, kinetic and thermodynamic parameters for the pairwise interactions among the three proteins were measured via two independent techniques, biolayer interferometry and latex nanoparticle-enhanced turbidimetry. The results obtained clearly indicate that LF is able to bind the ACE2 receptor ectodomain with significantly high affinity, whereas no binding to the RBD was observed up to the maximum "physiological" lactoferrin concentration range. Lactoferrin, above 1 µM concentration, thus appears to directly interfere with RBD-ACE2 binding, bringing about a measurable, up to 300-fold increase of the K
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In particular, kinetic and thermodynamic parameters for the pairwise interactions among the three proteins were measured via two independent techniques, biolayer interferometry and latex nanoparticle-enhanced turbidimetry. The results obtained clearly indicate that LF is able to bind the ACE2 receptor ectodomain with significantly high affinity, whereas no binding to the RBD was observed up to the maximum "physiological" lactoferrin concentration range. Lactoferrin, above 1 µM concentration, thus appears to directly interfere with RBD-ACE2 binding, bringing about a measurable, up to 300-fold increase of the K
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| subjects | ACE2 Angiotensin Angiotensin-converting enzyme 2 Binding Binding sites Biosensors Complex formation Coronaviruses COVID-19 Domains Glycoproteins Interferometry Investigations Lactoferrin Latex Nanoparticles Peptidyl-dipeptidase A Proteins Severe acute respiratory syndrome coronavirus 2 Viruses |
| title | Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain |
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