Mesoporous peptide frameworks engineered from crystallizable collagen-mimetic peptide amphiphiles.

“Mesoporous peptide frameworks engineered from crystallizable collagen-mimetic peptide amphiphiles. Perez AR(1), Liu J(2), Sikder SMM(1), Maity A(1), Adewole A(1), Oakden J(3), Ren G(2), Dutagaci B(3)(4), Merg AD(5). Author information: (1)Department of Chemistry and Biochemistry, University of California, Merced, Merced, CA, USA. (2)The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. (3)Department of Molecular and Cell Biology, University of California, Merced, Merced, CA, USA. (4)Health Sciences Research Institute, University of California, Merced, Merced, CA, USA. (5)Department of Chemistry and Biochemistry, University of California, Merced, Merced, CA, USA. amerg@ucmerced.edu. The rational design of porous frameworks with tunable pore dimensions and chemical functionalities is a critical step toward their implementation in diverse applications. While traditional porous materials are typically constructed from abiotic components, there is increasing interest in employing biologically derived building blocks (e.g., peptides and proteins) that offer unmatched structural and functional diversity. Here, we report the construction of crystalline mesoporous frameworks that are self-assembled from amphiphilic collagen-mimetic peptides. Comprehensive structural characterization via microscopy, spectroscopy, and computational techniques provides insights into the assembly packing model, in which hexagonally packed channels are interconnected by antiparallel-aligned collagen triple helices via hydrophobic and electrostatic interactions. Lastly, we demonstrate the functional potential of aCMP frameworks through the encapsulation of various molecular guests, including doxorubicin, an anti-cancer drug. Overall, this work establishes a class of mesoporous frameworks, derived from synthetically engineerable peptide conjugates, marking a significant step forward in broadening the architectural scope and application potential of peptide-based materials. © 2026. The Author(s). Conflict of interest statement: Competing interests: The authors declare no competing interests.”