CHARACTERISTICS OF GELATIN FROM SWIM BLADDER OF YELLOWFIN TUNA (THUNNUS ALBACORES) AS INFLUENCED BY EXTRACTING TEMPERATURES

Gelatin was extracted from the swim bladder of yellowfin tuna (Thunnus albacores) at different temperatures (60, 70 and 80°C) with the extraction yields of 35.6%, 41.1% and 47.3% (dryweight basis), respectively. The α-chains of gelatin decreased with increasing extraction temperatures.Similar amino acid compositions were noticeable among all gelatins, in which glycine constituted the major amino acid. Imino acids ranged from 169 to 172 residues/1,000 residues. Thegel strength of gelatin extracted at lower temperature was higher than that of gelatins extracted at higher temperatures. Gelling and melting temperatures for swim bladder gelatin were 11.07-15.24 and 20.36-22.33°C, respectively. Higher gelling and melting points were observed for gelatin extracted at lower temperatures. Microstructure of gel of gelatin extracted at 60°C was finerwith smaller voids, compared with others. FTIR spectra of obtained gelatins revealed the significant loss of molecular order of the triple-helix. Thus, extraction temperatures showed the directimpact on characteristics of gelatin from swim bladder

Fc-binding antibody-recruiting molecules exploit endogenous antibodies for anti-tumor immune responses

Redirecting endogenous antibodies in the bloodstream to tumor cells using synthetic molecules is a promising approach to trigger anti-tumor immune responses. However, current molecular designs only enable the use of a small fraction of endogenous antibodies, limiting the therapeutic potential. Here, we report Fc-binding antibody-recruiting molecules (Fc-ARMs) as the first example addressing this issue. Fc-ARMs are composed of an Fc-binding peptide and a targeting ligand, enabling the exploitation of endogenous antibodies through constant affinity to the Fc region of antibodies, whose sequence is conserved in contrast to the Fab region. We show that Fc-ARM targeting folate receptor-α (FR-α) redirects a clinically used antibody mixture to FR-α+ cancer cells, resulting in cancer cell lysis by natural killer cells in vitro. Fc-ARMs successfully interacted with antibodies in vivo and accumulated in tumors. Furthermore, Fc-ARMs recruited antibodies to suppress tumor growth in a mouse model. Thus, Fc-ARMs have the potential to be a novel class of cancer immunotherapeutic agents