{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T10:09:01Z","timestamp":1782122941308,"version":"3.54.5"},"reference-count":67,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T00:00:00Z","timestamp":1768262400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Capsaicin, a naturally occurring polyphenol, is known to affect energy expenditure and muscle fatigue and modulate contractions in skeletal muscle. The L-type Ca2+ channels are known to be an important ion channel involved in the various muscle functions and the effect of capsaicin on the skeletal L-type Ca2+ channels is currently unknown. In this study, the effects of capsaicin and capsaicin analogs on depolarization-induced Ca2+ effluxes through L-type Ca2+ channels in transverse tubule membranes from rabbit skeletal muscle and L-type Ca2+ currents recorded using the whole-cell patch clamp technique in rat myotubes were examined. Capsaicin, in the concentration range of 3\u2013100 \u00b5M, inhibited depolarization-induced Ca2+ effluxes. The effect of capsaicin was not reversed by TRPV1 antagonist SB-366791 (10 \u00b5M). While vanilloids (30 \u00b5M) including vanillin, vanillyl alcohol, and vanillylamine were ineffective, other capsaicinoids (30 \u00b5M) including dihydrocapsaicin, nonivamide, and nordihydrocapsaicin significantly inhibited Ca2+ effluxes, suggesting that hydrocarbon chains are required for inhibition. In rat myotubes, capsaicin inhibited L-type Ca2+ currents with an IC50 value of 27.2 \u03bcM in the presence of SB-366791. Furthermore, in docking studies and molecular dynamic simulations, capsaicinoids with an aliphatic tail showed stronger binding and stable bent conformations in CaV1.1, forming hydrogen bonds with Ser1011 and Thr935 and hydrophobic\/\u03c0\u2013alkyl contacts with Phe1008, Ile1052, Met1366, and Ala1369, resembling the binding mode of amlodipine. In conclusion, the results indicate that the function of L-type Ca2+ channels in mammalian skeletal muscle was inhibited by capsaicin and capsaicin analogs in a TRPV1-independent manner.<\/jats:p>","DOI":"10.3390\/biom16010135","type":"journal-article","created":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T08:17:32Z","timestamp":1768292252000},"page":"135","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Direct Effects of Capsaicin on Voltage-Dependent Calcium Channels of Mammalian Skeletal Muscle"],"prefix":"10.3390","volume":"16","author":[{"given":"Dmytro","family":"Isaev","sequence":"first","affiliation":[{"name":"Department of Cellular Membranology, Bogomoletz Institute of Physiology, 01024 Kiev, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatiana","family":"Prytkova","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Schmid College of Science and Technology, Chapman University, One University Drive, Orange, CA 92866, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Badarunnisa","family":"Mohamed","sequence":"additional","affiliation":[{"name":"Research Core Facility, Faculty of Medicine, Kuwait University, Safat 13110, Kuwait"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8873-660X","authenticated-orcid":false,"given":"Mohamed Omar","family":"Mahgoub","sequence":"additional","affiliation":[{"name":"Department of Health Sciences, College of Natural and Health Sciences, Zayed University, Abu Dhabi 144534, United Arab Emirates"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3231-6291","authenticated-orcid":false,"given":"Keun-Hang Susan","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Schmid College of Science and Technology, Chapman University, One University Drive, Orange, CA 92866, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6789-0085","authenticated-orcid":false,"given":"Murat","family":"Oz","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Therapeutics, College of Pharmacy, Kuwait University, Safat 13110, Kuwait"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,1,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2167569","DOI":"10.1080\/19336950.2023.2167569","article-title":"Advances in CaV1.1 gating: New insights into permeation and voltage-sensing mechanisms","volume":"17","author":"Bibollet","year":"2023","journal-title":"Channels"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/978-3-319-55858-5_2","article-title":"Structure-Function Relationship of the Voltage-Gated Calcium Channel Cav1.1 Complex","volume":"981","author":"Wu","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1038\/s41467-017-00629-x","article-title":"The Ca2+ influx through the mammalian skeletal muscle dihydropyridine receptor is irrelevant for muscle performance","volume":"8","author":"Dayal","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1038\/298292a0","article-title":"Slow inward calcium currents have no obvious role in muscle excitation-contraction coupling","volume":"298","author":"Lathrop","year":"1982","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1085\/jgp.200810105","article-title":"The skeletal L-type Ca2+ current is a major contributor to excitation-coupled Ca2+ entry","volume":"133","author":"Bannister","year":"2009","journal-title":"J. Gen. Physiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/S0022-3565(25)24724-3","article-title":"Decrease in the size of tetanic responses produced by nitrendipine or by extracellular calcium ion removal without blocking twitches or action potentials in skeletal muscle","volume":"257","author":"Oz","year":"1991","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1139\/y93-075","article-title":"Voltage-dependent calcium fluxes in skeletal muscle transverse tubule membranes in the range of late afterpotentials","volume":"71","author":"Oz","year":"1993","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/s13395-014-0027-1","article-title":"Ca2+ permeation and\/or binding to CaV1.1 fine-tunes skeletal muscle Ca2+ signaling to sustain muscle function","volume":"5","author":"Lee","year":"2015","journal-title":"Skelet. Muscle"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e15675","DOI":"10.14814\/phy2.15675","article-title":"Voltage sensor current, SR Ca2+ release, and Ca2+ channel current during trains of action potential-like depolarizations of skeletal muscle fibers","volume":"11","author":"Bibollet","year":"2023","journal-title":"Physiol. Rep."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"4781","DOI":"10.1113\/JP270252","article-title":"Voltage-gated Ca2+ influx through L-type channels contributes to sarcoplasmic reticulum Ca2+ loading in skeletal muscle","volume":"593","author":"Robin","year":"2015","journal-title":"J. Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1113\/JP273423","article-title":"How and why are calcium currents curtailed in the skeletal muscle voltage-gated calcium channels?","volume":"595","author":"Flucher","year":"2017","journal-title":"J. Physiol."},{"key":"ref_12","first-page":"1547","article-title":"Restricting calcium currents is required for correct fiber type specification in skeletal muscle","volume":"143","author":"Sultana","year":"2016","journal-title":"Development"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"23751","DOI":"10.1074\/jbc.M115.643544","article-title":"Ca2+ Binding\/Permeation via Calcium Channel, CaV1.1, Regulates the Intracellular Distribution of the Fatty Acid Transport Protein, CD36, and Fatty Acid Metabolism","volume":"290","author":"Georgiou","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1038\/nn.2792","article-title":"Neuromuscular synaptic patterning requires the function of skeletal muscle dihydropyridine receptors","volume":"14","author":"Chen","year":"2011","journal-title":"Nat. Neurosci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3891","DOI":"10.1016\/j.celrep.2018.05.085","article-title":"Calcium Influx and Release Cooperatively Regulate AChR Patterning and Motor Axon Outgrowth during Neuromuscular Junction Formation","volume":"23","author":"Kaplan","year":"2018","journal-title":"Cell Rep."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Basith, S., Cui, M., Hong, S., and Choi, S. (2016). Harnessing the Therapeutic Potential of Capsaicin and Its Analogues in Pain and Other Diseases. Molecules, 21.","DOI":"10.3390\/molecules21080966"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Fattori, V., Hohmann, M.S., Rossaneis, A.C., Pinho-Ribeiro, F.A., and Verri, W.A. (2016). Capsaicin: Current Understanding of Its Mechanisms and Therapy of Pain and Other Pre-Clinical and Clinical Uses. Molecules, 21.","DOI":"10.3390\/molecules21070844"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s00232-014-9727-z","article-title":"Capsaicin and N-arachidonoyl-dopamine (NADA) decrease tension by activating both cannabinoid and vanilloid receptors in fast skeletal muscle fibers of the frog","volume":"248","author":"Trujillo","year":"2015","journal-title":"J. Membr. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Giuriato, G., Venturelli, M., Matias, A., Soares, E., Gaetgens, J., Frederick, K.A., and Ives, S.J. (2022). Capsaicin and Its Effect on Exercise Performance, Fatigue and Inflammation after Exercise. Nutrients, 14.","DOI":"10.3390\/nu14020232"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1002\/med.21945","article-title":"Transient receptor potential vanilloid 1 (TRPV1)-independent actions of capsaicin on cellular excitability and ion transport","volume":"43","author":"Oz","year":"2023","journal-title":"Med. Res. Rev."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"172411","DOI":"10.1016\/j.ejphar.2019.172411","article-title":"Capsaicin inhibits the function of \u03b17-nicotinic acetylcholine receptors expressed in Xenopus oocytes and rat hippocampal neurons","volume":"857","author":"Alzaabi","year":"2019","journal-title":"Eur. J. Pharmacol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Nebrisi, E.E., Prytkova, T., Lorke, D.E., Howarth, L., Alzaabi, A.H., Yang, K.S., Howarth, F.C., and Oz, M. (2020). Capsaicin Is a Negative Allosteric Modulator of the 5-HT3 Receptor. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.01274"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/j.1476-5381.1996.tb15680.x","article-title":"Effect of capsaicin and analogues on potassium and calcium currents and vanilloid receptors in Xenopus embryo spinal neurones","volume":"119","author":"Kuenzi","year":"1996","journal-title":"Br. J. Pharmacol."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Isaev, D., Yang, K.S., Shabbir, W., Howarth, F.C., and Oz, M. (2022). Capsaicin Inhibits Multiple Voltage-Gated Ion Channels in Rabbit Ventricular Cardiomyocytes in TRPV1-Independent Manner. Pharmaceuticals, 15.","DOI":"10.3390\/ph15101187"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0014-2999(00)00396-4","article-title":"Endogenous cannabinoid anandamide directly inhibits voltage-dependent Ca2+ fluxes in rabbit T-tubule membranes","volume":"404","author":"Oz","year":"2000","journal-title":"Eur. J. Pharmacol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"11053","DOI":"10.1016\/S0021-9258(18)60425-9","article-title":"Voltage-dependent calcium channels in skeletal muscle transverse tubules. Measurements of calcium efflux in membrane vesicles","volume":"264","author":"Dunn","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/BF00421083","article-title":"Morphological, immunological and biochemical characterization of purified transverse tubule membranes isolated from rabbit skeletal muscle","volume":"87","author":"Rosemblatt","year":"1989","journal-title":"Mol. Cell Biochem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ejphar.2004.08.052","article-title":"Differential effects of endogenous and synthetic cannabinoids on voltage-dependent calcium fluxes in rabbit T-tubule membranes: Comparison with fatty acids","volume":"502","author":"Oz","year":"2004","journal-title":"Eur. J. Pharmacol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0091-679X(08)60375-1","article-title":"Skeletal muscle cultures","volume":"52","author":"Neville","year":"1997","journal-title":"Methods Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.ejphar.2010.02.013","article-title":"The effects of anandamide transport inhibitor AM404 on voltage-dependent calcium channels","volume":"634","author":"Alptekin","year":"2010","journal-title":"Eur. J. Pharmacol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1242\/dev.117.3.1153","article-title":"Appearance and evolution of calcium currents and contraction during the early post-fusional stages of rat skeletal muscle cells developing in primary culture","volume":"117","author":"Cognard","year":"1993","journal-title":"Development"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3131","DOI":"10.1002\/anie.202011793","article-title":"Structural Basis of the Modulation of the Voltage-Gated Calcium Ion Channel Cav1.1 by Dihydropyridine Compounds*","volume":"60","author":"Gao","year":"2021","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"D1102","DOI":"10.1093\/nar\/gky1033","article-title":"PubChem 2019 update: Improved access to chemical data","volume":"47","author":"Kim","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2522","DOI":"10.1021\/acs.jcim.9b00269","article-title":"PACKMOL-Memgen: A Simple-To-Use, Generalized Workflow for Membrane-Protein-Lipid-Bilayer System Building","volume":"59","author":"Gohlke","year":"2019","journal-title":"J. Chem. Inf. Model."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The Amber biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J. Comput. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"6183","DOI":"10.1021\/acs.jcim.3c01153","article-title":"AmberTools","volume":"63","author":"Case","year":"2023","journal-title":"J. Chem. Inf. Model."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3084","DOI":"10.1021\/ct400341p","article-title":"PTRAJ and CPPTRAJ: Software for Processing and Analysis of Molecular Dynamics Trajectory Data","volume":"9","author":"Roe","year":"2013","journal-title":"J. Chem. Theory Comput."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0028-3908(03)00305-8","article-title":"Identification and characterisation of SB-366791, a potent and selective vanilloid receptor (VR1\/TRPV1) antagonist","volume":"46","author":"Gunthorpe","year":"2004","journal-title":"Neuropharmacology"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Lotteau, S., Ducreux, S., Romestaing, C., Legrand, C., and Van Coppenolle, F. (2013). Characterization of functional TRPV1 channels in the sarcoplasmic reticulum of mouse skeletal muscle. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0058673"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.bbrc.2005.05.016","article-title":"Vanilloid receptor expressed in the sarcoplasmic reticulum of rat skeletal muscle","volume":"332","author":"Xin","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1074\/jbc.273.2.957","article-title":"Molecular determinants of L-type Ca2+ channel inactivation. Segment exchange analysis of the carboxyl-terminal cytoplasmic motif encoded by exons 40-42 of the human alpha1C subunit gene","volume":"273","author":"Soldatov","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1007\/BF00374503","article-title":"A possible role of sarcoplasmic Ca2+ release in modulating the slow Ca2+ current of skeletal muscle","volume":"425","author":"Feldmeyer","year":"1993","journal-title":"Pflugers Arch."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1007\/s00424-007-0344-x","article-title":"Ca2+\/CaM-dependent inactivation of the skeletal muscle L-type Ca2+ channel (Cav1.1)","volume":"455","author":"Stroffekova","year":"2008","journal-title":"Pflugers Arch."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1038\/sj.bjp.0701272","article-title":"Capsazepine block of voltage-activated calcium channels in adult rat dorsal root ganglion neurones in culture","volume":"121","author":"Docherty","year":"1997","journal-title":"Br. J. Pharmacol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1021\/jm00068a014","article-title":"Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 1. The aromatic \u201cA-region\u201d","volume":"36","author":"Walpole","year":"1993","journal-title":"J. Med. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"12086","DOI":"10.1021\/acs.jpcb.5b05351","article-title":"Location, Partitioning Behavior, and Interaction of Capsaicin with Lipid Bilayer Membrane: Study Using Its Intrinsic Fluorescence","volume":"119","author":"Swain","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1080\/19336950.2022.2026015","article-title":"Capsaicin as an amphipathic modulator of NaV1.5 mechanosensitivity","volume":"16","author":"Cowan","year":"2022","journal-title":"Channels"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1124\/mol.105.013573","article-title":"Capsaicin regulates voltage-dependent sodium channels by altering lipid bilayer elasticity","volume":"68","author":"Lundbaek","year":"2005","journal-title":"Mol. Pharmacol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1788","DOI":"10.1021\/cb500086e","article-title":"Phytochemicals perturb membranes and promiscuously alter protein function","volume":"9","author":"Thakur","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0378-8741(01)00200-8","article-title":"Biphasic membrane effects of capsaicin, an active component in Capsicum species","volume":"75","author":"Tsuchiya","year":"2001","journal-title":"J. Ethnopharmacol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1021\/acschemneuro.5b00168","article-title":"Capsaicin Fluidifies the Membrane and Localizes Itself near the Lipid-Water Interface","volume":"6","author":"Torrecillas","year":"2015","journal-title":"ACS Chem. Neurosci."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Efimova, S.S., Zakharova, A.A., and Ostroumova, O.S. (2020). Alkaloids Modulate the Functioning of Ion Channels Produced by Antimicrobial Agents via an Influence on the Lipid Host. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.00537"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1007\/s00424-020-02368-3","article-title":"Skeletal muscle CaV1.1 channelopathies","volume":"472","author":"Flucher","year":"2020","journal-title":"Pflugers Arch."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1093\/hmg\/ddr568","article-title":"Muscle weakness in myotonic dystrophy associated with misregulated splicing and altered gating of CaV1.1 calcium channel","volume":"21","author":"Tang","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1111\/nan.12076","article-title":"Alternative splicing alterations of Ca2+ handling genes are associated with Ca2+ signal dysregulation in myotonic dystrophy type 1 (DM1) and type 2 (DM2) myotubes","volume":"40","author":"Santoro","year":"2014","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"e173576","DOI":"10.1172\/JCI173576","article-title":"Verapamil mitigates chloride and calcium bi-channelopathy in a myotonic dystrophy mouse model","volume":"134","author":"Cisco","year":"2024","journal-title":"J. Clin. Investig."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1136\/jnnp.50.2.199","article-title":"Nifedipine in the treatment of myotonia in myotonic dystrophy","volume":"50","author":"Grant","year":"1987","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1002\/mus.880050114","article-title":"The effects of diltiazem in dystrophic hamsters","volume":"5","author":"Bhattacharya","year":"1982","journal-title":"Muscle Nerve"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0022-510X(93)90070-F","article-title":"Regulation of membrane-mediated chronic muscle degeneration in dystrophic hamsters by calcium-channel blockers: Diltiazem, nifedipine and verapamil","volume":"115","author":"Johnson","year":"1993","journal-title":"J. Neurol. Sci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1002\/mus.21188","article-title":"Diltiazem and verapamil protect dystrophin-deficient muscle fibers of MDX mice from degeneration: A potential role in calcium buffering and sarcolemmal stability","volume":"39","author":"Matsumura","year":"2009","journal-title":"Muscle Nerve"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Altamirano, F., Valladares, D., Henr\u00edquez-Olgu\u00edn, C., Casas, M., L\u00f3pez, J.R., Allen, P.D., and Jaimovich, E. (2013). Nifedipine treatment reduces resting calcium concentration, oxidative and apoptotic gene expression, and improves muscle function in dystrophic mdx mice. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0081222"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.bcp.2005.05.034","article-title":"Protective effects of Ca2+ handling drugs against abnormal Ca2+ homeostasis and cell damage in myopathic skeletal muscle cells","volume":"70","author":"Iwata","year":"2005","journal-title":"Biochem. Pharmacol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.jconrel.2014.09.027","article-title":"Bioavailability of capsaicin and its implications for drug delivery","volume":"196","author":"Rollyson","year":"2014","journal-title":"J. Control. Release"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1124\/pr.112.006163","article-title":"Unravelling the mystery of capsaicin: A tool to understand and treat pain","volume":"64","author":"Brock","year":"2012","journal-title":"Pharmacol. Rev."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1159\/000362740","article-title":"Cutaneous drug delivery of capsaicin after in vitro administration of the 8% capsaicin dermal patch system","volume":"28","author":"Wohlrab","year":"2015","journal-title":"Skin. Pharmacol. Physiol."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/1\/135\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T08:46:53Z","timestamp":1768294013000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/1\/135"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1,13]]},"references-count":67,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,1]]}},"alternative-id":["biom16010135"],"URL":"https:\/\/doi.org\/10.3390\/biom16010135","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,1,13]]}}}