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Its active ingredient is an altered peptide ligand\u2014derived from a T\u2010cell epitope of the human 60\u2010kDa heat shock protein\u2014referred to as CIGB\u2010814. Jusvinza has also proven effective in reducing hyperinflammation in COVID\u201019. However, molecular targets of CIGB\u2010814 in patients remain undefined, and this study is aimed at identifying specific plasma proteins that interact with CIGB\u2010814. Affinity chromatography and mass spectrometry analysis revealed apolipoprotein A\u2010I as a CIGB\u2010814\u2010binding partner. Interestingly, no apolipoprotein A\u2010I bands were detected in the affinity matrix of the wild\u2010type peptide (designated as E18\u20103). In this context, it was relevant to analyze how the substitution of Asp18 with Leu\u2014used to design CIGB\u2010814 from the wild\u2010type peptide\u2014confers its ability to bind apolipoprotein A\u2010I. Docking studies predicted the N\u2010terminal domain of apolipoprotein A\u2010I as the most likely region for peptide interaction and suggested a strong connection between CIGB\u2010814 and apolipoprotein A\u2010I. Further validation by molecular dynamics simulations suggests that CIGB\u2010814 may enhance the flexibility of structural areas in apolipoprotein A\u2010I critical for high\u2010density lipoproteins assembly. Additionally, an affinity enzyme\u2010linked immunosorbent assay (ELISA) confirmed that apolipoprotein A\u2010I has a tenfold greater affinity for CIGB\u2010814 compared to the wild\u2010type peptide. These integrated experimental and computational findings demonstrate that a single residue substitution is critical for apolipoprotein A\u2010I recognition. In addition, this study provides mechanistic insight into CIGB\u2010814 immunomodulatory and metabolic effects, expanding the therapeutic potential of Jusvinza to metabolic diseases associated with lipid homeostasis imbalance.<\/jats:p>","DOI":"10.1002\/psc.70113","type":"journal-article","created":{"date-parts":[[2026,7,3]],"date-time":"2026-07-03T14:18:21Z","timestamp":1783088301000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Apolipoprotein A\u2010I as a Molecular Target of the Immunomodulatory Peptide Jusvinza: Mechanistic Insights From Affinity and In Silico Studies"],"prefix":"10.1002","volume":"32","author":[{"given":"Camila Viviana","family":"Rosales","sequence":"first","affiliation":[{"name":"Autoinmmunity and Inflammation Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mabel Hern\u00e1ndez","family":"Cede\u00f1o","sequence":"additional","affiliation":[{"name":"Autoinmmunity and Inflammation Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Glay","family":"Chinea","sequence":"additional","affiliation":[{"name":"Bioinformatic Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir","family":"Besada","sequence":"additional","affiliation":[{"name":"Proteomic Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yassel","family":"Ramos","sequence":"additional","affiliation":[{"name":"Proteomic Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyung\u2010Hyun","family":"Cho","sequence":"additional","affiliation":[{"name":"Raydel Research Institute Medical Innovation Complex  Daegu Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Javier","family":"Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Proteomic Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gillian Mart\u00ednez","family":"Donato","sequence":"additional","affiliation":[{"name":"Autoinmmunity and Inflammation Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda","family":"del Carmen Dom\u00ednguez\u2010Horta","sequence":"additional","affiliation":[{"name":"Autoinmmunity and Inflammation Group, Biomedical Research Division Center for Genetic Engineering and Biotechnology  Playa La Habana Cuba"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,7,3]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2023.1162739"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.3109\/08916934.2010.550590"},{"key":"e_1_2_11_4_1","first-page":"153","article-title":"Therapeutic Effect of Two Altered Peptide Ligands Derived From the Human Heat Shock Protein 60 in Experimental Models of Rheumatoid Arthritis","volume":"30","author":"Dom\u00ednguez C. 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