This article reports theoretical values of target strength (TS) for mesopelagic lanternfishes based on morphological measurements of their swimbladders. Three species of lanternfishes, Diaphus theta (26.9–77.4 mm standard length (SL)), Symbolophorus californiensis (85.0–108.4 mm SL), and Notoscopelus japonicus (126.0–133.2 mm SL), were examined. After external morphological measurement of the fish body, a specialized “soft X-ray” imaging system was used to map the swimbladders and obtain their morphological parameters. The swimbladder was inflated in D. theta, uninflated in S. californiensis, and was absent in N. japonicus. For D. theta, the swimbladder length does not increase in proportion to the body length, suggesting that the contribution of the swimbladder to acoustic reflection is reduced with growth in this fish. Based on the morphological measurements, the theoretical TS of the fish at 38 kHz was calculated using the approximate deformed-cylinder model (DCM) and the general prolate-spheroid model (PSM). For all three species, the calculations showed about 3 dB difference between the TS indicated by the DCM and PSM. Given that the description of body shape is poor in PSM, the DCM results were adopted for fish without a swimbladder or an empty one. The intercept b20 in the standard formula TS = 20 log SL + b20 was −85.7 dB (DCM) for S. californiensis and −86.7 dB (DCM) for N. japonicus. On the other hand, the PSM model was adopted for D. theta since its swimbladder has too small an aspect ratio to apply the DCM. For D. theta, the relationship between SL and TS is best expressed by TS = 11.8 log SL − 63.5, which implies that its scattering cross-section is not proportional to the square of the body length.

The conjugation of biomolecules, such as protein, sugar, and DNA, with metal nanoparticles is an important technique for bioassay and biomaterial preparation. In this study, we aim to enzymatically immobilize a functional peptide on gold nanoparticles (AuNPs) using a single-step reaction. We used tyrosinase, a catechol oxidase, to immobilize an enzymatic peptide. We performed immobilization experiments of a fluorescent compound-linked caspase-3 substrate peptide using tyrosinase on chitosan-coated AuNPs. Peptides were effectively immobilized onto the AuNPs depending on the presence of tyrosine within the sequence, which suggests the DOPA-quinone produced from tyrosine, via tyrosinase, is connected to the chitosan amino group. Although fluorescent emission from the immobilized capase-3 substrate was quenched by AuNPs, fluorescence intensity recovery occurred due to the addition of caspase-3. Thus, we were able to easily prepare functional AuNPs that can be used for a caspase-3 activity assay. Our results indicate that the tyrosinase-mediated peptide link to chitosan-coated particles is a useful technique for preparing functionalized nanoparticles.

We produced a functional polymer whose framework comprised transthyretin (TTR) amyloid fibrils. In order to immobilize functional molecules onto the amyloid fibrils, transpeptidase sortase A (srtA), which catalyzes the covalent binding of LPXTG with polyglycine, was employed. After the preparation of the amyloid fibril of LPETGG-tagged TTR, immobilization of Gly5-fused GFP on the amyloid fibrils by srtA-mediated transpeptidation was carried out. SrtA recognized the amyloid fibrils consisting of an LPETGG-tagged TTR variant (L55P) as a good substrate, resulting in successful preparation of a GFP-immobilized amyloid. Intriguingly, the replacement of GFP with Gly5-fused luciferase was confirmed when the GFP-immobilized amyloids were mixed with Gly5-luciferase in the presence of srtA. Thus, it was found that functional molecules covalently immobilized on amyloid could be detached and substituted with other tagged molecules by using srtA.

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