---
title: "Heparin’s Concentration-Dependent Modulation of SARS-CoV-2 Spike–PF4 Interactions"
id: "pubmed-42607721"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42607721"
content_type: "clinical_feed_article"
specialty: "Critical Care"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42607721/"
doi: "10.1021/acsabm.6c00502"
published_at: "2026-09-07T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Heparin’s Concentration-Dependent Modulation of SARS-CoV-2 Spike–PF4 Interactions
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42607721
- **Specialty:** [Critical Care](https://medichelpline.com/clinical-feed/critical-care.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42607721/)
- **DOI:** [10.1021/acsabm.6c00502](https://doi.org/10.1021%2Facsabm.6c00502)
- **Published At:** 2026-09-07T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- The study examines how **heparin**, a highly sulfated glycosaminoglycan, affects interactions between the SARS-CoV-2 **spike protein** (S protein) and **platelet factor 4 (PF4)** using biochemical and biophysical approaches. - Methods included ensemble binding assays (ELISA), single-molecule force spectroscopy, and molecular dynamics simulations focusing on an unfractionated heparin (UFH) preparation and a dp5 heparin fragment. - **UFH** produced partner- and concentration-dependent effects: low UFH concentrations enhanced ACE2–S protein binding, while higher concentrations modestly reduced ACE2 engagement, indicating a biphasic effect on receptor binding. - For PF4–S protein interactions, UFH inhibited binding at low to intermediate concentrations, with partial restoration of binding at higher UFH levels. - Single-molecule force spectroscopy showed UFH decreased the mechanical stability of the PF4–S protein complex, demonstrated by reduced unbinding forces that saturated at concentrations ≥5 IU mL–1. - Molecular dynamics simulations with the dp5 fragment indicated favorable energetics for heparin binding to both PF4 and the S1 subunit of the spike protein. - In ternary S1–PF4–dp5 assemblies, heparin altered interfacial contacts and reshaped the energetic landscape, implying modulation via electrostatic reorganization and interface remodeling rather than simple competitive blockade. - Overall, the findings provide mechanistic insight into glycosaminoglycan-mediated regulation of PF4–S protein complexes and show that heparin can modulate viral–host protein interfaces in a concentration-dependent manner.
## Clinical Analysis & Structured Key Points
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Affiliations Expand ### Affiliations * 1 Institute for Bioprocessing and Analytical Measurement Techniques (iba), Heilbad Heiligenstadt37308, Germany. * 2 Faculty of Natural Sciences 1-Biosciences, Institute of Biology, Martin Luther University of Halle-Wittenberg, Halle06108, Germany. * 3 Laboratory for Computational Physics, Institute for Computational Science and Artificial Intelligence, Van Lang University, Ho Chi Minh City700000, Vietnam. * 4 Faculty of Mechanical, Electrical, and Computer Engineering, Van lang School of Technology, Van Lang University, Ho Chi Minh City700000, Vietnam. * 5 Faculty of Mathematics and Natural Sciences, Technische Universität Ilmenau, Ilmenau98694, Germany. * 6 Porelab, Department of Chemistry and Biomedical Science, Norwegian University of Science and Technology, Trondheim7491, Norway. * PMID: **42607721** * DOI: [ 10.1021/acsabm.6c00502 ](https://doi.org/10.1021/acsabm.6c00502) Item in Clipboard # Heparin Modulates SARS-CoV-2 Spike-Platelet Factor 4 Interactions through Concentration-Dependent Interface Remodeling Dayamai Sai Satram et al. ACS Appl Bio Mater. 2026. Show details Display options Display options Format Abstract PubMed PMID ACS Appl Bio Mater Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22ACS+Appl+Bio+Mater%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22ACS+Appl+Bio+Mater%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) . 2026 Sep 7;9(17):7999-8012. doi: 10.1021/acsabm.6c00502. ### Authors [Dayamai Sai Satram](https://pubmed.ncbi.nlm.nih.gov/?term=Satram+DS&cauthor_id=42607721)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-1 "Institute for Bioprocessing and Analytical Measurement Techniques \(iba\), Heilbad Heiligenstadt37308, Germany.")[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-2 "Faculty of Natural Sciences 1-Biosciences, Institute of Biology, Martin Luther University of Halle-Wittenberg, Halle06108, Germany."), [Li-Yu Chen](https://pubmed.ncbi.nlm.nih.gov/?term=Chen+LY&cauthor_id=42607721)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-1 "Institute for Bioprocessing and Analytical Measurement Techniques \(iba\), Heilbad Heiligenstadt37308, Germany."), [Thi H Ho](https://pubmed.ncbi.nlm.nih.gov/?term=Ho+TH&cauthor_id=42607721)[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-3 "Laboratory for Computational Physics, Institute for Computational Science and Artificial Intelligence, Van Lang University, Ho Chi Minh City700000, Vietnam.")[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-4 "Faculty of Mechanical, Electrical, and Computer Engineering, Van lang School of Technology, Van Lang University, Ho Chi Minh City700000, Vietnam."), [Doris Heinrich](https://pubmed.ncbi.nlm.nih.gov/?term=Heinrich+D&cauthor_id=42607721)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-1 "Institute for Bioprocessing and Analytical Measurement Techniques \(iba\), Heilbad Heiligenstadt37308, Germany.")[ 5 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-5 "Faculty of Mathematics and Natural Sciences, Technische Universität Ilmenau, Ilmenau98694, Germany."), [Thuat T Trinh](https://pubmed.ncbi.nlm.nih.gov/?term=Trinh+TT&cauthor_id=42607721)[ 6 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-6 "Porelab, Department of Chemistry and Biomedical Science, Norwegian University of Science and Technology, Trondheim7491, Norway."), [Thi-Huong Nguyen](https://pubmed.ncbi.nlm.nih.gov/?term=Nguyen+TH&cauthor_id=42607721)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-1 "Institute for Bioprocessing and Analytical Measurement Techniques \(iba\), Heilbad Heiligenstadt37308, Germany.")[ 5 ](https://pubmed.ncbi.nlm.nih.gov/42607721/#short-view-affiliation-5 "Faculty of Mathematics and Natural Sciences, Technische Universität Ilmenau, Ilmenau98694, Germany.") ### Affiliations * 1 Institute for Bioprocessing and Analytical Measurement Techniques (iba), Heilbad Heiligenstadt37308, Germany. * 2 Faculty of Natural Sciences 1-Biosciences, Institute of Biology, Martin Luther University of Halle-Wittenberg, Halle06108, Germany. * 3 Laboratory for Computational Physics, Institute for Computational Science and Artificial Intelligence, Van Lang University, Ho Chi Minh City700000, Vietnam. * 4 Faculty of Mechanical, Electrical, and Computer Engineering, Van lang School of Technology, Van Lang University, Ho Chi Minh City700000, Vietnam. * 5 Faculty of Mathematics and Natural Sciences, Technische Universität Ilmenau, Ilmenau98694, Germany. * 6 Porelab, Department of Chemistry and Biomedical Science, Norwegian University of Science and Technology, Trondheim7491, Norway. * PMID: **42607721** * DOI: [ 10.1021/acsabm.6c00502 ](https://doi.org/10.1021/acsabm.6c00502) Item in Clipboard Full text links Cite Display options Display options Format Abstract PubMed PMID ## Abstract Heparin, a highly sulfated glycosaminoglycan, interacts with numerous proteins through electrostatic and multivalent binding mechanisms. In the context of SARS-CoV-2 infection, platelet factor 4 (PF4) has been proposed to form complexes with the viral spike protein (S protein), potentially contributing to immune-mediated thrombotic complications. However, the molecular mechanisms by which heparin modulates PF4-S protein interactions remain poorly understood. Here, we investigate how unfractionated heparin (UFH) influences the formation and stability of PF4-S protein complexes using a combination of ensemble binding assays, single-molecule force spectroscopy, and molecular dynamics simulations. ELISA measurements reveal concentration-dependent and partner-specific effects of UFH on S protein interactions. While low concentrations of UFH enhance ACE2-S protein binding, higher concentrations produce a modest reduction, indicating biphasic modulation of receptor engagement. In contrast, UFH inhibits PF4-S protein binding at low to intermediate concentrations, with partial restoration at higher levels. Single-molecule force spectroscopy confirms that UFH decreases the mechanical stability of the PF4-S protein complex, as reflected by reduced unbinding forces that reach saturation at concentrations ≥5 IU mL-1. Molecular dynamics simulations using the dp5 heparin fragment demonstrate energetically favorable binding to both PF4 and the S1 subunit of the S protein. In ternary S1-PF4-dp5 assemblies, heparin alters interfacial contacts and reshapes the energetic landscape of the protein-protein interaction, suggesting modulation through electrostatic reorganization and interfacial remodeling. These findings provide mechanistic insight into glycosaminoglycan-mediated regulation of PF4-S protein complexes and highlight how heparin can modulate biomacromolecular interactions at viral-host protein interfaces. **Keywords:** SARS-CoV-2 spike protein; heparin; molecular dynamics simulation; platelet factor 4; protein-protein interactions; single-molecule force spectroscopy. © 2026 The Authors. Published by American Chemical Society. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## MeSH terms * COVID-19 / metabolism Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22COVID-19%2Fmetabolism%22%5BMeSH%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=COVID-19) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * COVID-19 / virology Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22COVID-19%2Fvirology%22%5BMeSH%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=COVID-19) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Heparin* / chemistry Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Heparin%2Fchemistry%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Heparin) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Heparin* / metabolism Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Heparin%2Fmetabolism%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Heparin) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Heparin* / pharmacology Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Heparin%2Fpharmacology%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Heparin) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Humans Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Humans%22%5BMeSH%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Humans) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Molecular Dynamics Simulation Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Molecular+Dynamics+Simulation%22%5BMeSH%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Molecular+Dynamics+Simulation) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Platelet Factor 4* / chemistry Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Platelet+Factor+4%2Fchemistry%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Platelet+Factor+4) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Platelet Factor 4* / metabolism Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Platelet+Factor+4%2Fmetabolism%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Platelet+Factor+4) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Protein Binding / drug effects Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Protein+Binding%2Fdrug+effects%22%5BMeSH%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=Protein+Binding) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * SARS-CoV-2* / metabolism Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22SARS-CoV-2%2Fmetabolism%22%5BMAJR%5D&sort=date&sort_order=desc) * [ Search in MeSH ](https://www.ncbi.nlm.nih.gov/mesh?term=SARS-CoV-2) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42607721/) * Spike Glycoprotein, Coronavirus* / chemistry Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22Spike+Glycoprotein%2C+Coronavir
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