ArticleMicromachines2026
A Multifunctional Peptide Linker Stably Anchors to Silica Spicules and Enables MMP-Responsive Release of Diverse Bioactive Cargos.
Article in Micromachines, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
11 authors.
Funding
Abstract
Silica spicules provide a natural transdermal conduit but require a linker that binds strongly under physiological conditions and releases payloads selectively in response to biological cues. Existing silane chemistries or polydopamine coatings lack enzyme responsiveness and show limited control over release. We created a 180-member peptide library with the motif L-X1-X2-[Y-F-Y]-A-L-G-P-H-C and screened for silica binding. Biophysical assays (circular dichroism, ζ-potential, quartz crystal microbalance, atomic force microscopy) and molecular dynamics identified high-affinity binders. The lead, P176, was tested for matrix metalloprotease (MMP)-responsive cleavage. Conjugation and release of Vitamin C and Stigmasterol were analyzed by HPLC and Franz diffusion cells. P176 showed high silica affinity (~55 µg mg
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