Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide

Peptide – mediated biomineralization is an emerging and promising biomimetic approach for the synthesis of nanomaterials. This nature – inspired technique of producing inorganic nanostructures depends on the biomineralization peptide to control the shape and morphology of the prevailing inorganic na...

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Main Authors: Janairo, Jose Isagani B., Sakaguchi, Kazuyasu
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Published: Animo Repository 2018
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Online Access:https://animorepository.dlsu.edu.ph/faculty_research/2280
https://animorepository.dlsu.edu.ph/context/faculty_research/article/3279/type/native/viewcontent
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spelling oai:animorepository.dlsu.edu.ph:faculty_research-32792021-08-23T01:10:08Z Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide Janairo, Jose Isagani B. Sakaguchi, Kazuyasu Peptide – mediated biomineralization is an emerging and promising biomimetic approach for the synthesis of nanomaterials. This nature – inspired technique of producing inorganic nanostructures depends on the biomineralization peptide to control the shape and morphology of the prevailing inorganic nanostructure. One of the challenges in peptide – mediated biomineralization is controlling the 3D arrangement and orientation of the peptide. Recently, we have developed a peptide platform that can specify and direct the geometric arrangement and spatial orientation of the biomineralization peptide. The peptide platform is composed of two segments: a metal binding sequence, and the tetramerization domain of the tumor suppressor p53 protein, which acts as the oligomerization control element. The resulting fusion peptide exhibits a spatially – fixed and well – controlled assembly of the palladium binding sequence. This present study demonstrates the utility and efficacy of this peptide platform to bimetallic materials. Monodispersed 5 nm bimetallic PdAg nanoparticles were synthesized using the oligomerization – controlled biomineralization peptide. The synthesis was carried out in an aqueous environment, void of harsh reagents. When other fusion biomineralization peptides were used to synthesize bimetallic PdAg nanoparticles, less ordered nanoparticles were yielded. The results highlight the importance of controlled assembly on bimetallic nanoparticle formation through biomineralization. The presented method offers a straightforward manner of creating monodispersed and extremely small nanoparticles, which are useful in a wide array of applications. © 2018 Trans Tech Publications, Switzerland. 2018-01-01T08:00:00Z text text/html https://animorepository.dlsu.edu.ph/faculty_research/2280 https://animorepository.dlsu.edu.ph/context/faculty_research/article/3279/type/native/viewcontent Faculty Research Work Animo Repository Biomimetics Bioinorganic chemistry Peptides Tumor suppressor proteins Chemical Engineering
institution De La Salle University
building De La Salle University Library
continent Asia
country Philippines
Philippines
content_provider De La Salle University Library
collection DLSU Institutional Repository
topic Biomimetics
Bioinorganic chemistry
Peptides
Tumor suppressor proteins
Chemical Engineering
spellingShingle Biomimetics
Bioinorganic chemistry
Peptides
Tumor suppressor proteins
Chemical Engineering
Janairo, Jose Isagani B.
Sakaguchi, Kazuyasu
Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
description Peptide – mediated biomineralization is an emerging and promising biomimetic approach for the synthesis of nanomaterials. This nature – inspired technique of producing inorganic nanostructures depends on the biomineralization peptide to control the shape and morphology of the prevailing inorganic nanostructure. One of the challenges in peptide – mediated biomineralization is controlling the 3D arrangement and orientation of the peptide. Recently, we have developed a peptide platform that can specify and direct the geometric arrangement and spatial orientation of the biomineralization peptide. The peptide platform is composed of two segments: a metal binding sequence, and the tetramerization domain of the tumor suppressor p53 protein, which acts as the oligomerization control element. The resulting fusion peptide exhibits a spatially – fixed and well – controlled assembly of the palladium binding sequence. This present study demonstrates the utility and efficacy of this peptide platform to bimetallic materials. Monodispersed 5 nm bimetallic PdAg nanoparticles were synthesized using the oligomerization – controlled biomineralization peptide. The synthesis was carried out in an aqueous environment, void of harsh reagents. When other fusion biomineralization peptides were used to synthesize bimetallic PdAg nanoparticles, less ordered nanoparticles were yielded. The results highlight the importance of controlled assembly on bimetallic nanoparticle formation through biomineralization. The presented method offers a straightforward manner of creating monodispersed and extremely small nanoparticles, which are useful in a wide array of applications. © 2018 Trans Tech Publications, Switzerland.
format text
author Janairo, Jose Isagani B.
Sakaguchi, Kazuyasu
author_facet Janairo, Jose Isagani B.
Sakaguchi, Kazuyasu
author_sort Janairo, Jose Isagani B.
title Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
title_short Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
title_full Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
title_fullStr Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
title_full_unstemmed Synthesis of bimetallic PdAg nanoparticles through an oligomerization-controlled biomineralization peptide
title_sort synthesis of bimetallic pdag nanoparticles through an oligomerization-controlled biomineralization peptide
publisher Animo Repository
publishDate 2018
url https://animorepository.dlsu.edu.ph/faculty_research/2280
https://animorepository.dlsu.edu.ph/context/faculty_research/article/3279/type/native/viewcontent
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