Presentation Information
[P04-541]Biomineralization Peptide Sequence–Programmed Liposomal Nanoreactors for Morphological Control of Gold Nanoparticles
○YUYA ABE1, Masayoshi Tanaka1 (1. Institute of Science Tokyo (Japan))
Keywords:
gold nanoparticles,liposomes,biomineralization peptides
[Purpose]
Liposome-based nanoreactors have attracted attention as platforms for controlled synthesis of metallic nanoparticles, including gold nanoparticles (AuNPs). In such confined systems, nucleation and growth can be regulated due to the limited number of reactants. 1 However, precise morphological control remains challenging with conventional reducing agents due to the lack of shape-directing capability. We have identified biomineralization peptides with dual functions: reduction of Au3+ and control of AuNP morphology. 2,3 However, selective formation of anisotropic AuNPs, such as triangular nanoplates, remains difficult in bulk solution due to multiple nucleation pathways. Here, we aimed to achieve controlled green synthesis of AuNPs by combining liposome nanoreactors with biomineralization peptides.
[Method]
Biomineralization peptides in tris-buffered saline were added to lipid films (DOPC:DOPE or DOPC:DOPE:DOTAP) to form multilamellar liposomes, followed by extrusion to obtain small unilamellar vesicles. After dialysis to remove free peptides, gold precursors were added to initiate nanoparticle formation. Au–liposome complexes were characterized by TEM, EDX, HRTEM, and confocal microscopy.
[Results]
A peptide known to produce triangular Au nanoplates in bulk solution yielded highly branched Au–liposome complexes. EDX and HRTEM confirmed their Au composition and polycrystalline nature. In contrast, a peptide producing ~2 nm AuNPs generated morphologies similar to bulk, with particles forming near lipid membranes regardless of liposome presence. Confocal microscopy revealed that peptide localization depended on sequence and lipid composition. A clear correlation was observed between localization and morphology: membrane-localized peptides formed branched structures, whereas encapsulated peptides produced near-spherical AuNPs.
[Consideration]
Peptide localization is governed by peptide–lipid physicochemical properties. Electrically neutral systems favored membrane localization, whereas charged components promoted encapsulation, likely due to hydrophobic and electrostatic interactions. The absence of triangular nanoplates in liposomes suggests altered peptide dynamics in confined environments, where precursor influx and membrane interactions disrupt facet-selective growth.
[Conclusion]
AuNPs were synthesized in peptide-programmed liposome nanoreactors, with morphology governed by peptide sequence and localization. This system provides a programmable platform for AuNP synthesis and introduces a design concept in which nanoreactor interior and interface are functionally differentiated.
[References]
[1] J. R. Henriksen et al., Nanoscale 2020, 12, 22298
[2] M. Tanaka et al., Acta Biomater. 2021, 131, 519-531
[3] S. Saito et al., ACS Appl. Nano Mater. 2025, 8, 13227-13237
Liposome-based nanoreactors have attracted attention as platforms for controlled synthesis of metallic nanoparticles, including gold nanoparticles (AuNPs). In such confined systems, nucleation and growth can be regulated due to the limited number of reactants. 1 However, precise morphological control remains challenging with conventional reducing agents due to the lack of shape-directing capability. We have identified biomineralization peptides with dual functions: reduction of Au3+ and control of AuNP morphology. 2,3 However, selective formation of anisotropic AuNPs, such as triangular nanoplates, remains difficult in bulk solution due to multiple nucleation pathways. Here, we aimed to achieve controlled green synthesis of AuNPs by combining liposome nanoreactors with biomineralization peptides.
[Method]
Biomineralization peptides in tris-buffered saline were added to lipid films (DOPC:DOPE or DOPC:DOPE:DOTAP) to form multilamellar liposomes, followed by extrusion to obtain small unilamellar vesicles. After dialysis to remove free peptides, gold precursors were added to initiate nanoparticle formation. Au–liposome complexes were characterized by TEM, EDX, HRTEM, and confocal microscopy.
[Results]
A peptide known to produce triangular Au nanoplates in bulk solution yielded highly branched Au–liposome complexes. EDX and HRTEM confirmed their Au composition and polycrystalline nature. In contrast, a peptide producing ~2 nm AuNPs generated morphologies similar to bulk, with particles forming near lipid membranes regardless of liposome presence. Confocal microscopy revealed that peptide localization depended on sequence and lipid composition. A clear correlation was observed between localization and morphology: membrane-localized peptides formed branched structures, whereas encapsulated peptides produced near-spherical AuNPs.
[Consideration]
Peptide localization is governed by peptide–lipid physicochemical properties. Electrically neutral systems favored membrane localization, whereas charged components promoted encapsulation, likely due to hydrophobic and electrostatic interactions. The absence of triangular nanoplates in liposomes suggests altered peptide dynamics in confined environments, where precursor influx and membrane interactions disrupt facet-selective growth.
[Conclusion]
AuNPs were synthesized in peptide-programmed liposome nanoreactors, with morphology governed by peptide sequence and localization. This system provides a programmable platform for AuNP synthesis and introduces a design concept in which nanoreactor interior and interface are functionally differentiated.
[References]
[1] J. R. Henriksen et al., Nanoscale 2020, 12, 22298
[2] M. Tanaka et al., Acta Biomater. 2021, 131, 519-531
[3] S. Saito et al., ACS Appl. Nano Mater. 2025, 8, 13227-13237
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