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Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain.
Piacentini, Roberta; Centi, Laura; Miotto, Mattia; Milanetti, Edoardo; Di Rienzo, Lorenzo; Pitea, Martina; Piazza, Paolo; Ruocco, Giancarlo; Boffi, Alberto; Parisi, Giacomo.
  • Piacentini R; Department of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Centi L; Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
  • Miotto M; Department of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Milanetti E; Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
  • Di Rienzo L; Department of Physics, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Pitea M; Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
  • Piazza P; Department of Physics, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Ruocco G; Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
  • Boffi A; Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291, 00181 Rome, Italy.
  • Parisi G; D-Tails s.r.l., Via di Torre Rossa 66, 00165 Rome, Italy.
Int J Mol Sci ; 23(10)2022 May 13.
Article in English | MEDLINE | ID: covidwho-1855645
ABSTRACT
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 KD value relative to RBD-ACE2 complex formation.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 / Lactoferrin Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Ijms23105436

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Angiotensin-Converting Enzyme 2 / SARS-CoV-2 / COVID-19 / Lactoferrin Limits: Humans Language: English Year: 2022 Document Type: Article Affiliation country: Ijms23105436