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Using a machine learning (ML)\u2013guided design strategy based on the plectasin scaffold, a peptide library was generated and DC05 was identified as the most active analog. As a free peptide, DC05 inhibited the H37Rv strain with an MIC\n                    <jats:sub>90<\/jats:sub>\n                    of 12.46 \u00b1 0.06\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    , displayed low cytotoxicity in MRC\u20105 fibroblasts (IC\n                    <jats:sub>50<\/jats:sub>\n                    &gt;250\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    ) and J774A.1 macrophages (115.18 \u00b1 8.49\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    ), and increased ethidium bromide accumulation to levels comparable to verapamil, with minimal hemolysis up to 256\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    . DC05 was then encapsulated into mesoporous silica nanoparticles (MSN), yielding\u00a0(MSN@DC05) and further functionalized with tuftsin, a cell\u2010penetrating peptide (CPP)\u00a0(MSN\u2010CPP@DC05). In simulated pulmonary fluid at 0.5\u00a0mg mL\n                    <jats:sup>\u22121<\/jats:sup>\n                    , all formulations remained colloidally stable, with hydrodynamic diameters between 122 and 164\u00a0nm and low polydispersity. Adsorption onto MSN followed a Langmuir\u2010type profile (qmax 39.5 \u00b1 4.9\u00a0mg g\n                    <jats:sup>\u22121<\/jats:sup>\n                    ). Release was strongly dependent on the surrounding medium, showing rapid diffusion in simulated pulmonary fluid, slower release in simulated intestinal fluid, and almost no detectable peptide in simulated gastric fluid, where acid\u2010driven degradation is likely. Nanoencapsulation enhanced antimycobacterial potency, reducing the MIC\n                    <jats:sub>90<\/jats:sub>\n                    to 5.74 \u00b1 0.15\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    for MSN@DC05 and 4.13 \u00b1 0.64\u00a0\u00b5\n                    <jats:sc>m<\/jats:sc>\n                    for MSN\u2010CPP@DC05, while maintaining high viability in mammalian cells up to 500\u00a0\u00b5g mL\n                    <jats:sup>\u22121<\/jats:sup>\n                    in macrophages and 2000\u00a0\u00b5g mL\n                    <jats:sup>\u22121<\/jats:sup>\n                    in fibroblasts. Ames testing showed mutagenicity indices below 2, and\n                    <jats:italic>Galleria mellonella<\/jats:italic>\n                    assays at 2000\u00a0mg kg\n                    <jats:sup>\u22121<\/jats:sup>\n                    confirmed high survival. Scanning electron microscopy combined with molecular dynamics supported a membrane\u2010disruptive mechanism for MSN\u2010CPP@DC05. These results indicate that integrating ML\u2010guided peptide design with a functionalized mesoporous carrier improves intracellular delivery and antimycobacterial activity while maintaining favorable safety profiles.\n                  <\/jats:p>","DOI":"10.1002\/adhm.202504285","type":"journal-article","created":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T06:33:11Z","timestamp":1774852391000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Dual\u2010Peptide Nanoplatform: Mesoporous Silica Nanoparticles Functionalized With a Cell\u2010Penetrating Peptide and Loaded With Rationally Designed Antimicrobial Peptides for Tuberculosis Therapy"],"prefix":"10.1002","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6694-7991","authenticated-orcid":false,"given":"Christian S.","family":"Carnero Canales","sequence":"first","affiliation":[{"name":"Tuberculosis Research Laboratory School of 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