---
title: "Binding Affinity and Conformational Changes of Ca2+-Calmodulin with HIV-1 Matrix Peptides"
id: "biorxiv-1-affinity-and-conformations-of-ca2-calmodulin-bound-to-peptides-containing-the"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-1-affinity-and-conformations-of-ca2-calmodulin-bound-to-peptides-containing-the"
content_type: "clinical_feed_article"
specialty: "Infectious Disease"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1?rss=1"
published_at: "2026-10-24T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Binding Affinity and Conformational Changes of Ca2+-Calmodulin with HIV-1 Matrix Peptides
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-1-affinity-and-conformations-of-ca2-calmodulin-bound-to-peptides-containing-the
- **Specialty:** [Infectious Disease](https://medichelpline.com/clinical-feed/infectious-disease.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1?rss=1)
- **Published At:** 2026-10-24T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The study measured interactions between synthetic peptides from the HIV-1 **MA** (matrix) protein and calcium-loaded **calmodulin** (**Ca2+-CaM**) using ensemble FRET and DEER spectroscopy. - Investigators used three Cy3-labeled MA peptide constructs: full-length wild type (FL WT), a C-terminal truncation lacking the KKK cluster, and a triple mutant K26N/K27H/K28Q; FL CaM S39C was labeled with Cy5 for FRET assays. - Binding affinities (dissociation constants) from eFRET were reported as approximately 80 nM (FL WT), ~65 nM (truncation), and ~250 nM (triple mutant), indicating stable complexes and a modest energetic penalty for the triple substitution. - Reported binding free energies ranged approximately from 9 to 9.8 kcal/mol across constructs; the authors concluded the central KKK cluster contributes little to Ca2+-CaM binding affinity. - DEER distance distributions for Ca2+-CaM labeled at S39C and A103C shifted on FL WT MA binding from an extended interspin distance (~5.3 nm) to a broader ~1.8–3 nm distribution, indicating major CaM restructuring upon peptide engagement. - The data indicate specific, high-affinity interactions between the MA CaM-binding motif and **Ca2+-CaM**, and show conformational remodeling of CaM when bound to MA peptides. - The source did not report cellular or in vivo validation, high-resolution atomic structures, nor kinetic rate constants for association/dissociation beyond the equilibrium affinities given. - Authors noted that thermodynamic and structural characterization helps clarify how **HIV-1** proteins exploit **calmodulin**, but the mechanistic role of CaM in viral trafficking in cells remains to be defined by further studies.
## Clinical Analysis & Structured Key Points
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Borbat, [ View ORCID Profile](http://orcid.org/0000-0001-9980-5260)Elka R. Georgieva doi: https://doi.org/10.64898/2026.10.19.760223 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. Arvin Saffarian Delkhosh 1 Texas Tech University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Arvin%2BSaffarian%2BDelkhosh%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Saffarian%20Delkhosh%20A&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AArvin%2BSaffarian%2BDelkhosh%2B) Adeyemi Ogunbowale 1 Texas Tech University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Adeyemi%2BOgunbowale%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Ogunbowale%20A&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AAdeyemi%2BOgunbowale%2B) Elaheh Hadadianpour 1 Texas Tech University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Elaheh%2BHadadianpour%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Hadadianpour%20E&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AElaheh%2BHadadianpour%2B) Kazi Mustafa Mahmud 1 Texas Tech University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Kazi%2BMustafa%2BMahmud%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Mahmud%20KM&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AKazi%2BMustafa%2BMahmud%2B) Peter P. Borbat 2 Cornell University * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Peter%2BP.%2BBorbat%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Borbat%20PP&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3APeter%2BP.%2BBorbat%2B) Elka R. Georgieva 1 Texas Tech University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Elka%2BR.%2BGeorgieva%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Georgieva%20ER&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AElka%2BR.%2BGeorgieva%2B) * [ORCID record for Elka R. Georgieva](http://orcid.org/0000-0001-9980-5260 "Open in new tab") * For correspondence: elgeorgi@ttu.edu * [Abstract](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5900174/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5900174/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5900174/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5900174/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5900174/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract Background: Protein-protein interactions enable viruses to adapt and replicate by modifying host factors. Thermodynamic characterization of viral-host complexes can reveal viral mechanisms, broader principles of protein interactions, and properties relevant to anti-HIV-1 inhibitor development. Here, we examine the binding of the HIV-1 matrix (MA) protein to host calmodulin (CaM). MA, the N-terminal domain of Gag (group-specific antigen), directs Gag to the plasma membrane for viral assembly and maturation and may recruit CaM to facilitate this trafficking. However, the MA-CaM interaction remains poorly characterized. MA contains a noncanonical N-terminal CaM-binding motif with hydrophobic regions that may mediate CaM binding and a central, positively charged KKK cluster. Objective: We aimed to determine the binding affinities of MA to calcium-bound CaM (Ca2+-CaM), elucidate protein regions that are critical to the heterocomplex formation, and monitor the conformational alterations in Ca2+-CaM upon binding to MA. Methods: We studied Ca2+-CaM binding to synthetic MA peptides representing full-length wild type (FL WT), a C-terminal truncation lacking the KKK cluster, and an FL K26N/K27H/K28Q triple mutant of the MA CaM-binding motif. The peptides were C-terminally labeled with Cy3, and FL CaM S39C with Cy5. Binding affinity was measured by ensemble Forster resonance energy transfer (eFRET) using 100 nM Cy3-MA and increasing Cy5-Ca2+-CaM concentrations in the range of 50 nM to 2.5 microM. Conformational changes in doubly spin-labeled Ca2+-CaM upon MA binding were probed by double electron-electron resonance (DEER) spectroscopy. Results: Cy3 quenching and FRET analyses of complexes with Cy5-Ca2+-CaM yielded dissociation constants of ~80 nM for FL WT MA, ~65 nM for the truncation, and ~250 nM for the triple mutant, with corresponding binding free energies of ~9.8 to ~9 kcal/mol. These values indicate stable, specific complexes and show that the KKK cluster contributes little to MA-Ca2+-CaM binding. DEER measurements of Ca2+-CaM labeled at S39C and A103C showed that FL WT MA binding shifted the ~5.3 nm interspin distance of extended Ca2+-CaM to a broader ~1.8-3 nm distribution, indicating a major CaM restructuring. Conclusion: These findings define key energetic and structural features of MA-Ca2+-CaM interactions and clarify how HIV-1 proteins exploit CaM. ### Competing Interest Statement The authors have declared no competing interest. ## Funder Information Declared Gilead Sciences (United States) National Institutes of Health, 5R24GM146107 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY-NC-ND 4.0 International license](http://creativecommons.org/licenses/by-nc-nd/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. [Donate to openRxiv ](https://www.zeffy.com/en-US/donation-form/donate-to-make-a-difference-10981) [ Back to top](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1?rss=1#page) [ Previous](https://www.biorxiv.org/content/10.64898/2026.10.19.760258v1 "When are population connectome harmonics adequate representations of individual brains?") Posted October 24, 2026. [ Download PDF](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.full.pdf) Print/Save Options [Download PDF](https://www.biorxiv.org/content/biorxiv/early/2026/10/24/2026.10.19.760223.full.pdf)Full Text & In-line FiguresXML [More Info](https://www.biorxiv.org/about/FAQ#PrintOptions "More Information on Print/Save Options") [Supplementary Material ](https://www.biorxiv.org/content/10.64898/2026.10.19.760223v1.supplementary-material) [ Email](https://www.biorxiv.org/ "Email this Article") [ Share](https://www.biorxiv.org/) Affinity and Conformations of Ca2+-Calmodulin Bound to Peptides Containing the Calmodulin-Binding Motif of HIV-1 Matrix Protein Arvin Saffarian Delkhosh, Adeyemi Ogunbowale, Elaheh Hadadianpour, Kazi Mustafa Mahmud, Peter P. Borbat, Elka R. Georgieva bioRxiv 2026.10.19.760223; doi: https://doi.org/10.64898/2026.10.19.760223 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. 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