Anti-FH monoclonal antibody, clone 4F8

In the present study, we evaluated new sources of plant proteases from fruits ofBromelia karatas(BK) andBromelia pinguin(BP) to obtain antioxidant hydrolyzates/bioactive peptides (BPs) derived from chicken by-products (CH) and fish by-products (FH). The profile of the peptides was identified by reverse-phase high-resolution liquid chromatography (RP-HPLC) and the size weight distribution by molecular exclusion chromatography (SEC). The hydrolysates obtained with BK in both sources of by-products showed greater antioxidant capacity compared to those obtained with BP, presenting similar or higher values when compared to a commercial plant enzyme. The use of new sources of plant proteases allowed to obtain hydrolysates of hydrophilic character with a high percentage (> 50%) of peptides with molecular weights < 17.5 kDa from chicken and fish by-products. Therefore, based on the results obtained in antioxidant capacity it is possible to consider the hydrolysates as potential ingredients, food additives, and pharmaceutical products.

Inhibition of the complement activation has emerged as an option for treatment of a range of diseases. Activation of the lectin and alternative pathways (LP and AP, respectively) contribute to the deterioration of conditions in certain diseases such as ischemia-reperfusion injuries and age-related macular degeneration (AMD). In the current study, we generated dual complement inhibitors of the pathways MAp44-FH and sMAP-FH by fusing full-length MAp44 or small mannose-binding lectin-associated protein (sMAP), LP regulators, with the N-terminal five short consensus repeat (SCR) domains of complement factor H (SCR1/5-FH), an AP regulator. The murine forms of both fusion proteins formed a complex with endogenous mannose-binding lectin (MBL) or ficolin A in the circulation when administered in mice intraperitoneally. Multiple complement activation assays revealed that sMAP-FH had significantly higher inhibitory effects on activation of the LP and AP in vivo as well as in vitro compared to MAp44-FH. Human form of sMAP-FH also showed dual inhibitory effects on LP and AP activation in human sera. Our results indicate that the novel fusion protein sMAP-FH inhibits both the LP and AP activation in mice and in human sera, and could be an effective therapeutic agent for diseases in which both the LP and AP activation are significantly involved.