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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Questions
  9. Schema
  10. External Links
  11. Analytics And Tracking
  12. Libraries
  13. CDN Services

We are analyzing https://link.springer.com/article/10.1007/s12551-025-01276-z.

Title:
Biophysics of SARS-CoV-2 spike protein’s receptor-binding domain interaction with ACE2 and neutralizing antibodies: from computation to functional insights | Biophysical Reviews
Description:
The spike protein encoded by the SARS-CoV-2 has become one of the most studied macromolecules in recent years due to its central role in COVID-19 pathogenesis. The spike protein’s receptor-binding domain (RBD) directly interacts with the host-encoded receptor protein, ACE2. This review critically examines computational insights into RBD’s interaction with ACE2 and with therapeutic antibodies designed to interfere with this interaction. We begin by summarizing insights from early computational studies on pre-pandemic SARS-CoV-1 RBD interactions and how these early studies shaped the understanding of SARS-CoV-2. Next, we highlight key theoretical contributions that revealed the molecular mechanisms behind the binding affinity of SARS-CoV-2 RBD against ACE2, and the structural changes that have enhanced the infectivity of emerging variants. Special attention is given to the “RBD charge rule”, a predictive framework for determining variant infectivity based on the electrostatic properties of the RBD. Towards applying the computational insights to therapy, we discuss a multiscale computational protocol for optimizing monoclonal antibodies to improve binding affinity across multiple spike protein variants, including representatives from the Omicron family. Finally, we explore how these insights can inform the development of future vaccines and therapeutic interventions for combating future coronavirus diseases.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • Books & Literature

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {💸}

We can't see how the site brings in money.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

retrieved, sarscov, protein, publisher, spike, ace, chem, nature, binding, receptor, article, coronavirus, human, httpsdoiorgs, publishing, httpsdoiorg, antibody, pubmed, molecular, zhang, rbd, sci, computational, variants, wang, antibodies, group, silva, affinity, design, phys, american, httpsdoiorgacsjpcbc, domain, barroso, interactions, society, receptorbinding, covid, science, google, scholar, httpswwwnaturecomarticless, cell, chemical, dynamics, structure, cas, mol, rev,

Topics {✒️}

org/social-issues-migration-health/healthat-a-glance-latin-america org/en/content/articlelanding/2018/cs/c8cs00523k org/content/article/scienceadviserfinding-hope-long gov/pmc/articles/pmc7755986/ xie gov/articles/pmc2992757/ bayarri-olmos /science/article/pii/s0092867422011199 tai /science/article/pii/s0021925820751112 wrapp gov/pmc/articles/pmc8266303/ dai gov/pmc/articles/pmc9693616/ geng /science/article/pii/007961079290006r oecd /science/article/pii/s1359644622002823 vuitika gov/pmc/articles/pmc2242497/ convertino sars-cov-2 receptor-binding domain gov/pmc/articles/pmc10183628/ wu /science/article/pii/s009286742030338x wang /science/article/pii/s1476927107000278 zhou month download article/chapter sars-cov-1/cov-2 spike proteins cn/en/article/doi/https /retrieve/pii/s0021925821003148 begum /retrieve/pii/s0006291x2401115x bò /retrieve/pii/s0168165605007492 gangavarapu /retrieve/pii/s0006291x03026792 prachar /retrieve/pii/s1532046414002330 sormanni /retrieve/pii/s0165614704000975 vabret /retrieve/pii/s1074761320301837 verma sars-cov-2 spike glycoprotein host species-specific receptors gov/articles/pmc9115176/ schymkowitz aleea grigore ghica-voda sars-cov-2 spike protein sars-cov-2 spike protein angiotensin-converting enzyme 2 sars-cov-2 omicron subvariants antibody complementarity-determining regions high-density repetitive manner receptor-binding domain interaction molecular dynamics-based approach /retrieve/pii/s0092867420302622 wang cryo-electron microscopy structures vlp-based covid-19 vaccines sars-cov-2 omicron xbb sars-cov-2 spike proteins sars-cov-2 spike rbd omicron sars-cov-2 rbd constant-ph simulation methods high-throughput molecular simulations host-encoded receptor protein sars-cov2—molecular design updates including sabdab-nano

Questions {❓}

  • Batlle D, Soler MJ, Ye M (2010) ACE2 and Diabetes: ACE of ACEs?
  • Nguyen HL, Lan PD, Thai NQ, Nissley DA, O’Brien EP, Li MS (2020) Does SARS-CoV-2 Bind to Human ACE2 More Strongly Than Does SARS-CoV?
  • Spinello A, Saltalamacchia A, Magistrato A (2020) Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity?
  • De Andrade J, Gonçalves PFB, Netz PA (2021) Why Does the Novel Coronavirus Spike Protein Interact so Strongly with the Human ACE2?
  • Org/plosone/article?
  • Org/plospathogens/article?

Schema {🗺️}

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         headline:Biophysics of SARS-CoV-2 spike protein’s receptor-binding domain interaction with ACE2 and neutralizing antibodies: from computation to functional insights
         description:The spike protein encoded by the SARS-CoV-2 has become one of the most studied macromolecules in recent years due to its central role in COVID-19 pathogenesis. The spike protein’s receptor-binding domain (RBD) directly interacts with the host-encoded receptor protein, ACE2. This review critically examines computational insights into RBD’s interaction with ACE2 and with therapeutic antibodies designed to interfere with this interaction. We begin by summarizing insights from early computational studies on pre-pandemic SARS-CoV-1 RBD interactions and how these early studies shaped the understanding of SARS-CoV-2. Next, we highlight key theoretical contributions that revealed the molecular mechanisms behind the binding affinity of SARS-CoV-2 RBD against ACE2, and the structural changes that have enhanced the infectivity of emerging variants. Special attention is given to the “RBD charge rule”, a predictive framework for determining variant infectivity based on the electrostatic properties of the RBD. Towards applying the computational insights to therapy, we discuss a multiscale computational protocol for optimizing monoclonal antibodies to improve binding affinity across multiple spike protein variants, including representatives from the Omicron family. Finally, we explore how these insights can inform the development of future vaccines and therapeutic interventions for combating future coronavirus diseases.
         datePublished:2025-03-08T00:00:00Z
         dateModified:2025-03-08T00:00:00Z
         pageStart:309
         pageEnd:333
         sameAs:https://doi.org/10.1007/s12551-025-01276-z
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            Electrostatic interactions
            pH effects
            Molecular simulation
            Complexation
            Antibodies
            Virus
            Transmissibility
            Biochemistry
            general
            Biological and Medical Physics
            Biophysics
            Cell Biology
            Membrane Biology
            Biological Techniques
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                        name:Department of Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
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                     name:Nanjing Tech University
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                        name:State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, People’s Republic of China
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                     name:Luleå University of Technology
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                        name:Department of Engineering Sciences and Mathematics, Division of Energy Science, Luleå University of Technology, Luleå, Sweden
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                     name:Aleea Grigore Ghica-Voda
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                        name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
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      headline:Biophysics of SARS-CoV-2 spike protein’s receptor-binding domain interaction with ACE2 and neutralizing antibodies: from computation to functional insights
      description:The spike protein encoded by the SARS-CoV-2 has become one of the most studied macromolecules in recent years due to its central role in COVID-19 pathogenesis. The spike protein’s receptor-binding domain (RBD) directly interacts with the host-encoded receptor protein, ACE2. This review critically examines computational insights into RBD’s interaction with ACE2 and with therapeutic antibodies designed to interfere with this interaction. We begin by summarizing insights from early computational studies on pre-pandemic SARS-CoV-1 RBD interactions and how these early studies shaped the understanding of SARS-CoV-2. Next, we highlight key theoretical contributions that revealed the molecular mechanisms behind the binding affinity of SARS-CoV-2 RBD against ACE2, and the structural changes that have enhanced the infectivity of emerging variants. Special attention is given to the “RBD charge rule”, a predictive framework for determining variant infectivity based on the electrostatic properties of the RBD. Towards applying the computational insights to therapy, we discuss a multiscale computational protocol for optimizing monoclonal antibodies to improve binding affinity across multiple spike protein variants, including representatives from the Omicron family. Finally, we explore how these insights can inform the development of future vaccines and therapeutic interventions for combating future coronavirus diseases.
      datePublished:2025-03-08T00:00:00Z
      dateModified:2025-03-08T00:00:00Z
      pageStart:309
      pageEnd:333
      sameAs:https://doi.org/10.1007/s12551-025-01276-z
      keywords:
         Electrostatic interactions
         pH effects
         Molecular simulation
         Complexation
         Antibodies
         Virus
         Transmissibility
         Biochemistry
         general
         Biological and Medical Physics
         Biophysics
         Cell Biology
         Membrane Biology
         Biological Techniques
         Nanotechnology
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         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Fernando Luís Barroso da Silva
            affiliation:
                  name:Universidade de São Paulo
                  address:
                     name:Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil
                     type:PostalAddress
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                  name:NC State University
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                     name:Department of Chemical and Biomolecular Engineering, NC State University, Raleigh, USA
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            name:Karen Paco
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                  name:Keck Graduate Institute
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                     name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Aatto Laaksonen
            affiliation:
                  name:Stockholm University
                  address:
                     name:Department of Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
                     type:PostalAddress
                  type:Organization
                  name:Nanjing Tech University
                  address:
                     name:State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, People’s Republic of China
                     type:PostalAddress
                  type:Organization
                  name:Luleå University of Technology
                  address:
                     name:Department of Engineering Sciences and Mathematics, Division of Energy Science, Luleå University of Technology, Luleå, Sweden
                     type:PostalAddress
                  type:Organization
                  name:Aleea Grigore Ghica-Voda
                  address:
                     name:Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, Iasi, Romania
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Animesh Ray
            affiliation:
                  name:Keck Graduate Institute
                  address:
                     name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
                     type:PostalAddress
                  type:Organization
                  name:California Institute of Technology
                  address:
                     name:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, USA
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                  type:Organization
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      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Universidade de São Paulo
      address:
         name:Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil
         type:PostalAddress
      name:NC State University
      address:
         name:Department of Chemical and Biomolecular Engineering, NC State University, Raleigh, USA
         type:PostalAddress
      name:Keck Graduate Institute
      address:
         name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
         type:PostalAddress
      name:Stockholm University
      address:
         name:Department of Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
         type:PostalAddress
      name:Nanjing Tech University
      address:
         name:State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, People’s Republic of China
         type:PostalAddress
      name:Luleå University of Technology
      address:
         name:Department of Engineering Sciences and Mathematics, Division of Energy Science, Luleå University of Technology, Luleå, Sweden
         type:PostalAddress
      name:Aleea Grigore Ghica-Voda
      address:
         name:Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, Iasi, Romania
         type:PostalAddress
      name:Keck Graduate Institute
      address:
         name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
         type:PostalAddress
      name:California Institute of Technology
      address:
         name:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, USA
         type:PostalAddress
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Person:
      name:Fernando Luís Barroso da Silva
      affiliation:
            name:Universidade de São Paulo
            address:
               name:Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil
               type:PostalAddress
            type:Organization
            name:NC State University
            address:
               name:Department of Chemical and Biomolecular Engineering, NC State University, Raleigh, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Karen Paco
      affiliation:
            name:Keck Graduate Institute
            address:
               name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
               type:PostalAddress
            type:Organization
      name:Aatto Laaksonen
      affiliation:
            name:Stockholm University
            address:
               name:Department of Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
               type:PostalAddress
            type:Organization
            name:Nanjing Tech University
            address:
               name:State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, People’s Republic of China
               type:PostalAddress
            type:Organization
            name:Luleå University of Technology
            address:
               name:Department of Engineering Sciences and Mathematics, Division of Energy Science, Luleå University of Technology, Luleå, Sweden
               type:PostalAddress
            type:Organization
            name:Aleea Grigore Ghica-Voda
            address:
               name:Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, Iasi, Romania
               type:PostalAddress
            type:Organization
      name:Animesh Ray
      affiliation:
            name:Keck Graduate Institute
            address:
               name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
               type:PostalAddress
            type:Organization
            name:California Institute of Technology
            address:
               name:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil
      name:Department of Chemical and Biomolecular Engineering, NC State University, Raleigh, USA
      name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
      name:Department of Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
      name:State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, People’s Republic of China
      name:Department of Engineering Sciences and Mathematics, Division of Energy Science, Luleå University of Technology, Luleå, Sweden
      name:Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, Iasi, Romania
      name:Riggs School of Applied Life Sciences, Keck Graduate Institute, Claremont, USA
      name:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, USA
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External Links {🔗}(368)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

5.1s.