α,ε-Hybrid Peptide-Stabilized Magnetic Nanoparticle-Coated Paper-Based Actuators

Abstract

The development of α,ε-hybrid peptide-stabilized magnetic nanoparticles and their application to fabricate a paper-based actuator has been reported. From single-crystal diffraction analysis, the nitropeptide 2 has an extended structure with a trans geometry. The one-pot in situ multiple oxidation–reduction reaction of a synthetic nitropeptide solution in ammonium hydroxide and FeCl2 leads to the formation of Fe3O4 nanoparticles. The reduction reaction replaces the nitro group with an amine group, which finally acts as capping agent for the stabilization of the Fe3O4 nanoparticles. Paper-based soft magneto machines with multivariant actuation modes such as contraction–expansion, bending, and uplifting locomotion have been studied. The device has potential as controllable paper-based soft robots.

Development of Novel Peptide-Modified Silver Nanoparticle-Based Rapid Biosensors for Detecting Aminoglycoside Antibiotics

“…However, the absence of an amide II peak at 1546 cm –1 suggests that bonding occurs between the CHPs and AgNPs via N–H bending and C–N stretching vibrations . Furthermore, the absence of an IR peak in the 1450–1400 cm –1 range indicates the possible involvement of π–π interactions and hydrogen bonding between the CHPs and AgNPs. , An IR peak at 1160 cm –1 matches with stretching vibrations, and the C–O single bond reveals the possibility of ligand exchange, enabling the CHPs to chemisorb onto the surface of AgNPs . Overall, the FTIR results indicate that the capping of AgNP surfaces can be achieved through multiple functionalities, including amine, carboxyl, and hydroxyl groups present in the peptides.…”

“…74,75 An IR peak at 1160 cm −1 matches with stretching vibrations, and the C−O single bond reveals the possibility of ligand exchange, enabling the CHPs to chemisorb onto the surface of AgNPs. 76 Overall, the FTIR results indicate that the capping of AgNP surfaces can be achieved through multiple functionalities, including amine, carboxyl, and hydroxyl groups present in the peptides.…”