RESUMEN
A novel ultrasonic micro linear motor that uses 1st longitudinal and 2nd bending modes, derived from a bartype stator with a rectangular slot cut through the stator length, has been proposed and designed for end-effect devices of microrobotics and bio-medical applications. The slot structure plays an important role in the motor design, and can be used not only to tune the resonance frequency of the two vibration modes but also to reduce the undesirable longitudinal coupling displacement caused by bending vibration at the end of the stator. By using finite element analysis, the optimal slot dimension to improve the driving tip motion was determined, resulting in the improvement of the motor performance. The trial linear motor, with a weight of 1.6 g, gave a maximum driving velocity of 1.12 m/s and a maximum driving force of 3.4 N. A maximum mechanical output power of 1.1 W was obtained at force of 1.63 N and velocity of 0.68 m/s. The output mechanical power per unit weight was 688 W/kg.
Asunto(s)
Microtecnología/instrumentación , Ultrasonografía/instrumentación , Análisis de Elementos Finitos , Fenómenos Mecánicos , RobóticaRESUMEN
Direct expression of lactoferricin, an antimicrobial peptide, is lethal to Escherichia coli. For the efficient production of lactoferricin in E. coli, we developed an expression system in which the gene for the lysine- and arginine-rich cationic lactoferricin was fused to an anionic peptide gene to neutralize the basic property of lactoferricin, and successfully overexpressed the concatemeric fusion gene in E. coli. The lactoferricin gene was linked to a modified magainin intervening sequence gene by a recombinational polymerase chain reaction, thus producing an acidic peptide-lactoferricin fusion gene. The monomeric acidic peptide-lactoferricin fusion gene was multimerized and expressed in E. coli BL21(DE3) upon induction with isopropyl-beta-D-thiogalactopyranoside. The expression levels of the fusion peptide reached the maximum at the tetramer, while further increases in the copy number of the fusion gene substantially reduced the peptide expression level. The fusion peptides were isolated and cleaved to generate the separate lactoferricin and acidic peptide. About 60 mg of pure recombinant lactoferricin was obtained from 1 L of E. coli culture. The purified recombinant lactoferricin was found to have a molecular weight similar to that of chemically synthesized lactoferricin. The recombinant lactoferricin showed antimicrobial activity and disrupted bacterial membrane permeability, as the native lactoferricin peptide does.