{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T09:19:39Z","timestamp":1787822379714,"version":"build-2784847793"},"reference-count":35,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T00:00:00Z","timestamp":1787788800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100018806","name":"Hubei Double Hundred Science and Technology Empowerment Project","doi-asserted-by":"publisher","award":["2025EIA078"],"award-info":[{"award-number":["2025EIA078"]}],"id":[{"id":"10.13039\/501100018806","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100018806","name":"special fund for central government guiding local science and technology development","doi-asserted-by":"publisher","award":["2025CSA104"],"award-info":[{"award-number":["2025CSA104"]}],"id":[{"id":"10.13039\/501100018806","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ningxia Hui Autonomous Region Natural Science Foundation project","award":["2026aac030681"],"award-info":[{"award-number":["2026aac030681"]}]},{"name":"Hubei Normal University 2023 Talent Introduction Project","award":["HS2023RC084"],"award-info":[{"award-number":["HS2023RC084"]}]},{"award":["HS2023RC084"],"award-info":[{"award-number":["HS2023RC084"]}],"id":[{"id":"https:\/\/ror.org\/056y3dw16","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Foods"],"abstract":"<jats:p>Lipid peroxidation products can induce oxidative modification of myofibrillar proteins (MPs), thereby compromising their water-holding capacity (WHC), but the underlying molecular mechanism remains unclear. This study systematically investigated the mechanism of MDA-induced WHC deterioration in bovine myofibrillar proteins (MPs) using multispectral techniques, redox proteomics, and molecular docking. Results demonstrated that low MDA concentrations caused relatively limited water release. Structural alterations became evident at 2 mM, whereas pronounced WHC deterioration occurred at 5\u201310 mM. At these higher concentrations, centrifugal loss increased by up to 48.80%, and immobilized water migrated to free water (p &lt; 0.05). This functional decline was accompanied by substantial structural remodeling, characterized by a transition from \u03b1-helix to \u03b2-sheet conformations, decreased hydrogen bonding, and enhanced disulfide-associated cross-linking. Furthermore, redox proteomics identified 581 differential cysteine redox sites, including 343 increased and 238 decreased sites. Among these sites, 57 markedly decreased sites associated with myofibrillar and cytoskeletal proteins were further characterized, including sites in actin, \u03b1-actinin, myosin, and LIM-domain-containing proteins. Motif analysis further revealed a characteristic cysteine-rich C-x-x-C-x-C sequence pattern surrounding responsive oxidation sites. Molecular docking of 12 representative cysteine sites supported the spatial feasibility of MDA pre-association near these cysteine-containing regions, with actin C258 exhibiting the most negative docking score among the examined sites (\u22123.3 kcal\/mol). These findings reveal that cysteine redox remodeling was associated with structural reorganization and increased water mobility, thereby contributing to WHC deterioration.<\/jats:p>","DOI":"10.3390\/foods15173022","type":"journal-article","created":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T08:02:27Z","timestamp":1787817747000},"page":"3022","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Mechanism of Malondialdehyde-Induced Deterioration in Water-Holding Capacity of Bovine Myofibrillar Proteins: Insights from Structural Modifications and Molecular Docking"],"prefix":"10.3390","volume":"15","author":[{"given":"He","family":"Li","sequence":"first","affiliation":[{"name":"College of Life Sciences, Hubei Normal University, Huangshi 435002, China"},{"name":"College of Food Science and Engineering, Hainan University, Haikou 570228, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhenyu","family":"Fang","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Hubei Normal University, Huangshi 435002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qin","family":"Wu","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Hubei Normal University, Huangshi 435002, China"},{"name":"College of Fisheries, Huazhong Agricultural University, Wuhan 430070, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dunhua","family":"Liu","sequence":"additional","affiliation":[{"name":"College of Food Science and Engineering, Ningxia University, Yinchuan 750021, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Liu","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Hubei Normal University, Huangshi 435002, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ningxia","family":"Bu","sequence":"additional","affiliation":[{"name":"Ningxia Veterinary Drugs and Fodder Inspection Institute, Yinchuan 750011, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"101913","DOI":"10.1016\/j.fochx.2024.101913","article-title":"Study on the effects of pre-slaughter transport stress on water holding capacity of pork: Insights from oxidation, structure, function, and degradation properties of protein","volume":"24","author":"Ma","year":"2024","journal-title":"Food Chem. X"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"5370","DOI":"10.1111\/1541-4337.12845","article-title":"Drying dynamics of meat highlighting areas of relevance to dry-aging of beef","volume":"20","author":"Hamill","year":"2021","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"114357","DOI":"10.1016\/j.foodres.2024.114357","article-title":"Myofibrillar protein lipoxidation in fish induced by linoleic acid and 4-hydroxy-2-nonenal: Insights from LC-MS\/MS analysis","volume":"187","author":"Feng","year":"2024","journal-title":"Food Res. Int."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"N\u00e8gre-Salvayre, A., and Salvayre, R. (2024). Reactive carbonyl species and protein lipoxidation in atherogenesis. Antioxidants, 13.","DOI":"10.3390\/antiox13020232"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"11809","DOI":"10.1080\/10408398.2023.2245029","article-title":"Interrelationship of lipid aldehydes (MDA, 4-HNE, and 4-ONE) mediated protein oxidation in muscle foods","volume":"64","author":"Huang","year":"2024","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"102146","DOI":"10.1016\/j.fochx.2024.102146","article-title":"Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications","volume":"25","author":"Li","year":"2025","journal-title":"Food Chem. X"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"100304","DOI":"10.1016\/j.fochx.2022.100304","article-title":"Haem-mediated protein oxidation affects water-holding capacity of beef during refrigerated storage","volume":"14","author":"Liu","year":"2022","journal-title":"Food Chem. X"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Yin, Y., Zhou, L., Cai, J., Feng, F., Xing, L., and Zhang, W. (2022). Effect of malondialdehyde on the digestibility of beef myofibrillar protein: Potential mechanisms from structure to modification site. Foods, 11.","DOI":"10.3390\/foods11152176"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/s41538-026-00869-6","article-title":"Differential oxidation of surimi actomyosin by malondialdehyde and heme: Spectroscopy and molecular simulation","volume":"10","author":"Zhu","year":"2026","journal-title":"npj Sci. Food"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"138563","DOI":"10.1016\/j.foodchem.2024.138563","article-title":"Effect of MDA-mediated oxidation on the protein structure and digestive properties of golden pomfret","volume":"443","author":"Chen","year":"2024","journal-title":"Food Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.foodchem.2019.02.126","article-title":"Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat","volume":"288","author":"Wang","year":"2019","journal-title":"Food Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"118688","DOI":"10.1016\/j.foodres.2026.118688","article-title":"Insights into the salt-mediated effect of oat \u03b2-glucan on lamb myofibrillar protein gels: Integrated multiscale characterization and molecular simulations","volume":"231","author":"Wang","year":"2026","journal-title":"Food Res. Int."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"106488","DOI":"10.1016\/j.psj.2026.106488","article-title":"Transcriptomics and metabolomics provide insights into meat flavor precursor differences between different duck lines","volume":"105","author":"Li","year":"2026","journal-title":"Poult. Sci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0304-4165(93)90003-Q","article-title":"The reaction of malondialdehyde with lens proteins and the protective effect of aspirin","volume":"1158","author":"Harding","year":"1993","journal-title":"Biochim. Biophys. Acta-Gen. Subj."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"149232","DOI":"10.1016\/j.foodchem.2026.149232","article-title":"Metabolic profiling of different developmental stages of Coriandrum sativum L. leaves using 1H-nuclear magnetic resonance spectroscopy","volume":"516","author":"Patil","year":"2026","journal-title":"Food Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"142612","DOI":"10.1016\/j.foodchem.2024.142612","article-title":"An integrated approach based on UHPLC-HRMS, 1H-NMR and sensory analysis reveals the exclusive lipid fingerprint of long-ripened protected designation of origin Coppa Piacentina","volume":"469","author":"Rocchetti","year":"2025","journal-title":"Food Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1002\/mnfr.201000453","article-title":"Protein oxidation in muscle foods: A review","volume":"55","author":"Lund","year":"2011","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"3766","DOI":"10.1021\/jf505916f","article-title":"Controlled formation of emulsion gels stabilized by salted myofibrillar protein under malondialdehyde (MDA)-induced oxidative stress","volume":"63","author":"Zhou","year":"2015","journal-title":"J. Agric. Food Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3564","DOI":"10.1080\/10408398.2018.1498444","article-title":"Effects of protein oxidation on the texture and water-holding of meat: A review","volume":"59","author":"Bao","year":"2019","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.meatsci.2017.09.011","article-title":"Myofibrillar protein oxidation affects filament charges, aggregation and water-holding","volume":"135","author":"Bao","year":"2018","journal-title":"Meat Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"e71008","DOI":"10.1111\/1750-3841.71008","article-title":"Comparison of Oxidation Extent, Structural Changes, and Oxidation Modification Types of Myofibrillar Protein Treated by Hydroxyl Radical and Peroxyalkyl Radical Oxidation System","volume":"91","author":"Tang","year":"2026","journal-title":"J. Food Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"139567","DOI":"10.1016\/j.foodchem.2024.139567","article-title":"Myofibrillar protein hydrolysis under hydroxyl radical oxidative stress: Structural changes and their impacts on binding to selected aldehydes","volume":"452","author":"Hu","year":"2024","journal-title":"Food Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"101448","DOI":"10.1016\/j.fochx.2024.101448","article-title":"Effects of different protein cross-linking degrees on physicochemical and subsequent thermal gelling properties of silver carp myofibrillar proteins sol subjected to freeze-thaw cycles","volume":"22","author":"Ding","year":"2024","journal-title":"Food Chem. X"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1021\/cr300163e","article-title":"Cysteine-Mediated Redox Signaling: Chemistry, Biology,.and Tools for Discovery","volume":"113","author":"Paulsen","year":"2013","journal-title":"Chem. Rev."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"9706","DOI":"10.1021\/acs.jafc.1c03045","article-title":"Redox Proteomic Analysis Reveals Microwave-Induced Oxidation Modifications of Myofibrillar Proteins from Silver Carp. (Hypophthalmichthys molitrix)","volume":"69","author":"Jiao","year":"2021","journal-title":"J. Agric. Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"140173","DOI":"10.1016\/j.foodchem.2024.140173","article-title":"Unlocking the molecular modifications of plasma-activated water-induced oxidation through redox proteomics: In the case of duck myofibrillar protein (Anas platyrhynchos)","volume":"458","author":"Rao","year":"2024","journal-title":"Food Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"4404","DOI":"10.1073\/pnas.90.10.4404","article-title":"The LIM motif defines a specific zinc-binding protein domain","volume":"90","author":"Michelsen","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"104080","DOI":"10.1016\/j.fbio.2024.104080","article-title":"Exploring the impact of malondialdehyde and 4-hydroxy-2-nonena on myofibrillar protein structure: A proteomic analysis","volume":"59","author":"Zhu","year":"2024","journal-title":"Food Biosci."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Zhu, X., Ma, Z., Zhang, X., Huang, X., Liu, J., and Zhuang, X. (2022). Effect of Malondialdehyde-Induced Oxidation Modification on Physicochemical Changes and Gel Characteristics of Duck Myofibrillar Proteins. Gels, 8.","DOI":"10.20944\/preprints202209.0237.v1"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"19661","DOI":"10.1074\/jbc.274.28.19661","article-title":"Reactions of Lipid-derived Malondialdehyde with Collagen","volume":"274","author":"Slatter","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e70320","DOI":"10.1111\/1750-3841.70320","article-title":"Structural Changes and Molecular Mechanisms of Myosin Induced by Oxidative Modification With Malondialdehyde","volume":"90","author":"Cao","year":"2025","journal-title":"J. Food Sci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"115719","DOI":"10.1016\/j.lwt.2023.115719","article-title":"Effect of linoleic acid-induced oxidation on the water retention of golden pompano: Myoglobin and myofibrillar protein oxidation","volume":"192","author":"Xu","year":"2024","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"108679","DOI":"10.1016\/j.fbio.2026.108679","article-title":"Suppression of Lipid Oxidation in Frozen Unwashed Surimi by Polyphenols-extract of Foods: Investigating the Synergistic Mechanism of Targeting Hemoglobin and Key Radical-producing Enzymes","volume":"79","author":"Xiang","year":"2026","journal-title":"Food Biosci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"115519","DOI":"10.1016\/j.lwt.2023.115519","article-title":"The restorative role and mechanism of L-lysine in yak myofibrillar protein gelling properties under malondialdehyde-induced over-oxidation damage","volume":"189","author":"Lu","year":"2023","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.meatsci.2017.04.232","article-title":"Relationship between proteolysis and water-holding of myofibrils","volume":"131","author":"Zeng","year":"2017","journal-title":"Meat Sci."}],"container-title":["Foods"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2304-8158\/15\/17\/3022\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T08:35:04Z","timestamp":1787819704000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2304-8158\/15\/17\/3022"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,27]]},"references-count":35,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["foods15173022"],"URL":"https:\/\/doi.org\/10.3390\/foods15173022","relation":{},"ISSN":["2304-8158"],"issn-type":[{"value":"2304-8158","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,27]]}}}