Spectrally selective antireflection of nanoimprint lithography-formed 3D spherical structures on film coated with a silver layer.

We fabricate moth-eye antireflection (AR) coatings using high-resolution and low-cost UV nanoimprint lithography with polyethylene terphthalate (PET) molds. Several various thicknesses of silver films placed on the moth-eye structure were analyzed for reflectance and transmission. On PET, the conical nanostructured surface arrays had a spatial period length of approximately 250 nm, a diameter of approximately 200 nm, and a height of approximately 160 nm. After them, a silver (Ag) layer of 18 nm is deposited satisfactorily on the PET substrate surface. The never-ending moth-eye formations of the imprinted mold were fabricated by Ni mold electroplating, interference lithography, and replication. We found that an Ag layer of suitable thickness on AR film in the spectrum range that can be seen has high transmittance (Highest value is 72%) while in the infrared spectrum it has high reflectance (At least 60%). For an optical film with a silver coating has been placed on an anti-reflection subwavelength-structured (ASS) surface, such properties, including heat insulation, have obvious applications in windows for homes and vehicles.

Vaccination against gonadotropin-releasing hormone (GnRH) using toxin receptor-binding domain-conjugated GnRH repeats.

A method for the preparation of an immunogen containing multiple copies of a self-peptide in linear alignment was designed in order to overcome the difficulty of inducing an immune response to poorly immunogenic peptide antigens. DNA fragments encoding multiple repeats of the self-peptide were generated by a new technique, termed template-repeated polymerase chain reaction (TR-PCR), which could be subcloned into an expression vector for production of peptide repeats as an immunogen. This approach was tested by constructing fusion proteins containing the receptor-binding domain of Pseudomonas exotoxin A and multiple copies of the 10-residue sequence of the peptide hormone gonadotropin-releasing hormone (GnRH). Immunization of female rabbits with the immunogen that contained the exotoxin receptor-binding domain and 12 copies of GnRH (PEIa-GnRH12) resulted in the generation of high-titer antibodies specific for GnRH. Although at equal molar basis of the GnRH moiety, the immunogen that contained single copy of GnRH (PEIa-GnRH1) induced low-titer anti-GnRH antibodies. These observations suggest that the presence of multiple peptide repeats is a key factor in eliciting an immune response. In addition, anti-GnRH antibodies effectively neutralized GnRH activity in vivo, as demonstrated by the degeneration of the ovaries in the injected rabbits. Because anti-GnRH antibody could be functionally analogous to GnRH antagonist, which has been used to treat patients with ovarian cancer, vaccination of PEIa-GnRH12 presents a potential therapeutic application for the treatment of GnRH-sensitive ovarian cancer.