Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding Domain
Piacentini et al.,
Lactoferrin Inhibition of the Complex Formation between ACE2 Receptor and SARS CoV-2 Recognition Binding..,
International Journal of Molecular Sciences, doi:10.3390/ijms23105436 (In Vitro)
Biolayer interferometry and turbidimetry study showing lactoferrin inhibits ACE2 - SARS-CoV-2 RBD binding.
Piacentini et al., 13 May 2022, Italy, peer-reviewed, 10 authors.
Contact:
giacomo.parisi@iit.it (corresponding author), roberta.piacentini@uniroma1.it, centi.laura95@gmail.com, alberto.boffi@uniroma1.it, miottomattia1@gmail.com, edoardo.milanetti@uniroma1.it, lorenzo.dirienzo@iit.it, martina.pitea@iit.it, giancarlo.ruocco@iit.it, paolopiazza@edifinstruments.com.
In Vitro studies are an important part of preclinical research, however results may be very different in vivo.
Abstract: International Journal of
Molecular Sciences
Article
Lactoferrin Inhibition of the Complex Formation between ACE2
Receptor and SARS CoV-2 Recognition Binding Domain
Roberta Piacentini 1,2 , Laura Centi 1 , Mattia Miotto 2,3 , Edoardo Milanetti 2,3 , Lorenzo Di Rienzo 2 ,
Martina Pitea 2,4 , Paolo Piazza 5 , Giancarlo Ruocco 2,3 , Alberto Boffi 1 and Giacomo Parisi 2, *
1
2
3
4
5
*
Citation: Piacentini, R.; Centi, L.;
Miotto, M.; Milanetti, E.; Di Rienzo,
L.; Pitea, M.; Piazza, P.; Ruocco, G.;
Boffi, A.; Parisi, G. Lactoferrin
Department of Biochemistry, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy;
roberta.piacentini@uniroma1.it (R.P.); centi.laura95@gmail.com (L.C.); alberto.boffi@uniroma1.it (A.B.)
Center of Life Nano and Neuro Science, Institute of Italian Technology, Viale Regina Elena 291,
00181 Rome, Italy; miottomattia1@gmail.com (M.M.); edoardo.milanetti@uniroma1.it (E.M.);
lorenzo.dirienzo@iit.it (L.D.R.); martina.pitea@iit.it (M.P.); giancarlo.ruocco@iit.it (G.R.)
Department of Physics, Sapienza University, Piazzale Aldo Moro 5, 00185 Rome, Italy
D-Tails s.r.l., Via di Torre Rossa 66, 00165 Rome, Italy
EDIF Instruments s.r.l., Via Ardeatina 132, 00147 Rome, Italy; paolopiazza@edifinstruments.com
Correspondence: giacomo.parisi@iit.it
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.
Inhibition of the Complex Formation
between ACE2 Receptor and SARS
CoV-2 Recognition Binding Domain.
Keywords: SARS-CoV-2 receptor-binding domain (RBD); angiotensin-converting enzyme 2 (ACE2);
lactoferrin; biolayer interferometry; nanoparticle enhanced turbidimetry; kinetic analysis
Int. J. Mol. Sci. 2022, 23, 5436.
https://doi.org/10.3390/ijms23105436
Academic Editor: Samuel De Visser
Received: 20 April 2022
Accepted: 11 May 2022
Published: 13 May 2022
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