Dataset Information

Biomimetic Crystallization of MnFe2O4 Mediated by Peptide-Catalyzed Esterification at Low Temperature.

ABSTRACT: Enzymes are some of the most efficient catalysts in nature. If small catalytic peptides mimic enzymes, there is potential for broad applications from catalysis for new material synthesis to drug development, due to the ease of molecular design. Recently a hydrogel-based combinatory phage display library was developed and protease-mimicking peptides were identified. Here we advanced the previous discovery to apply one of these catalytic peptides for the synthesis of bimetal oxide nanocrystals through the catalytic ester-elimination pathway. Conventional bimetal oxide crystallization usually requires high temperatures above several hundred °C; however, this catalytic peptide could grow superparamagnetic MnFe2O4 nanocrystals at 4°C. Superconducting quantum interference device (SQUID) analysis revealed that MnFe2O4 nano-crystals grown by the catalytic peptide exhibit superpara-magnetism. This study demonstrates the usefulness of protease-mimicking catalytic peptides in the field of material synthesis.

SUBMITTER: Maeda Y

PROVIDER: S-EPMC6801106 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Biomimetic Crystallization of MnFe<sub>2</sub>O<sub>4</sub> Mediated by Peptide-Catalyzed Esterification at Low Temperature.

Maeda Yoshiaki Y Wei Zengyan Z Ikezoe Yasuhiro Y Tam Edmund E Matsui Hiroshi H

ChemNanoMat : chemistry of nanomaterials for energy, biology and more 20151123 5

Enzymes are some of the most efficient catalysts in nature. If small catalytic peptides mimic enzymes, there is potential for broad applications from catalysis for new material synthesis to drug development, due to the ease of molecular design. Recently a hydrogel-based combinatory phage display library was developed and protease-mimicking peptides were identified. Here we advanced the previous discovery to apply one of these catalytic peptides for the synthesis of bimetal oxide nanocrystals thr ...[more]

PMID: 31632896

Similar Datasets

Project description:We report here a novel biomimetic approach to the regeneration of human enamel. The approach combines the use of inorganic pyrophosphate (PPi) to control the onset and rate of enamel regeneration and the use of leucine-rich amelogenin peptide (LRAP), a nonphosphorylated 56-amino acid alternative splice product of amelogenin, to regulate the shape and orientation of growing enamel crystals. This study builds on our previous findings that show LRAP can effectively guide the formation of ordered arrays of needle-like hydroxyapatite (HA) crystals in vitro and on the known role mineralization inhibitors, like PPi, play in the regulation of mineralized tissue formation. Acid-etched enamel surfaces of extracted human molars, cut perpendicular or parallel to the direction of the enamel rods, were exposed to a PPi-stabilized supersaturated calcium phosphate (CaP) solution containing 0 to 0.06 mg/mL LRAP for 20 h. In the absence of LRAP, PPi inhibition was reversed by the presence of etched enamel surfaces and led to the formation of large, randomly distributed plate-like HA crystals that were weakly attached, regardless of rod orientation. In the presence of 0.04 mg/mL LRAP, however, densely packed mineral layers, comprising bundles of small needle-like HA crystals, formed on etched surfaces that were cut perpendicular to the enamel rods. These crystals were strongly attached, and their arrangement reflected to a significant degree the underlying enamel prism pattern. In contrast, under the same conditions with LRAP, little to no crystal formation was found on enamel surfaces that were cut parallel to the direction of the enamel rods. These results suggest that LRAP preferentially interacts with ab surfaces of mature enamel crystals, inhibiting their directional growth, thus selectively promoting linear growth along the c-axis of enamel crystals. The present findings demonstrate a potential for the development of a new approach to regenerate enamel structure and properties.

Dataset Information

Biomimetic Crystallization of MnFe2O4 Mediated by Peptide-Catalyzed Esterification at Low Temperature.

Publications

Biomimetic Crystallization of MnFe<sub>2</sub>O<sub>4</sub> Mediated by Peptide-Catalyzed Esterification at Low Temperature.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets