{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T19:35:12Z","timestamp":1793129712464,"version":"4.5.0"},"posted":{"date-parts":[[2026,6,22]]},"group-title":"Biophysics","reference-count":66,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T00:00:00Z","timestamp":1782086400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,10,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  The cardiac \u03b2-myosin (MYH7) variant E525K was identified in 2012 in a patient with dilated cardiomyopathy (DCM). Work using engineered myosin constructs has shown that this variant stabilizes the interacting heads motif (IHM) of myosin and increases the ATPase activity of variant motor S1 heads. However, no measurements have been made in myofilaments or cardiomyocytes to determine its effect on contractile function. Here, we present force and contractile kinetics measurements from induced pluripotent stem cell-derived cardiomyocytes (iPSC-CMs) gene-edited for heterozygous expression of the E525K variant. Single-cell contraction for E525K hiPSC-CMs was reduced by 65%, and isometric twitch force in engineered heart tissues (EHTs) was reduced by 39%. In contrast, maximal Ca\n                  <jats:sup>2+<\/jats:sup>\n                  activated isometric force in isolated myofibrils was increased by 45%, and sub-maximal Ca\n                  <jats:sup>2+<\/jats:sup>\n                  activated force was similar to that of WT myofibrils. Structural analysis revealed reduced myofibril content (13.7% decrease) and decreased organization (increased z-disk dispersion angle) in E525K cells. We confirmed that E525K S1 myosin has higher actin affinity than WT S1 and elevated ATPase activity. However, there was no change in S1 ADP release rate. There was also no change in either the rate of force development or relaxation in myofibrils, cells, or EHTs. These findings suggest that E525K myosin crossbridge cycling is not altered during loaded contractions. To understand how the twitch force of myocytes decreased while the maximal isometric force increased, we used a spatially explicit, stochastic-kinetic sarcomere model. The results were explained by changes in three rates: reduced recruitment from the OFF\/IHM state and increased rates of actin binding and Pi release. Finite element modeling was used to demonstrate that additional contractile deficits in cells and EHTs likely result from myofibrillar disorganization. This study demonstrates the value of multi-scale analysis and coupled computational modeling for understanding the molecular mechanisms underlying sarcomere mutations in cardiomyocytes.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>Graphical Abstract<\/jats:title>\n                  <jats:fig id=\"ufig1\" position=\"float\" orientation=\"portrait\" fig-type=\"figure\">\n                    <jats:label>Graphical Abstract:<\/jats:label>\n                    <jats:caption>\n                      <jats:title>A model for how the hypothesized effects of the E525K mutation impact contracting myofibrils<\/jats:title>\n                      <jats:p>Here, we show that the E525K mutation impacts contraction in multiple ways: (1) Decreased sarcomere organization in cells and tissues drives decreased force generation. (2) Increased binding affinity of E525K myosin for actin and faster Pi release contribute to increased force generation in isolated myofibrils. (3) Increased IHM stability reduces twitch force. (4) The rate-limiting step of loaded crossbridge cycling, ADP release, is unchanged by the E525K mutation, and the rates of loaded contraction and relaxation are unchanged at all scales of contraction. Finally, a spatially explicit sarcomere model is used to demonstrate that these biochemical changes to myosin recruitment, binding, and cycling can explain force generation at tissue, cell, and myofibril levels.<\/jats:p>\n                    <\/jats:caption>\n                    <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"733270v3_ufig1\" position=\"float\" orientation=\"portrait\"\/>\n                  <\/jats:fig>\n                <\/jats:sec>","DOI":"10.64898\/2026.06.18.733270","type":"posted-content","created":{"date-parts":[[2026,6,23]],"date-time":"2026-06-23T04:25:18Z","timestamp":1782188718000},"source":"Crossref","is-referenced-by-count":1,"title":["The E525K \u03b2-Myosin Mutation Causes Hypocontractility in Cardiomyocytes Without Altering Crossbridge Cycling"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1577-8280","authenticated-orcid":false,"given":"Kalen 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