Modulation of biological motion perception in humans by gravity

The human visual perceptual system is highly sensitive to biological motion (BM) but less sensitive to its inverted counterpart. This perceptual inversion effect may stem from our selective sensitivity to gravity-constrained life motion signals and confer an adaptive advantage to creatures living on Earth. However, to what extent and how such selective sensitivity is shaped by the Earth&#39;s gravitational field is heretofore unexplored. Taking advantage of a spaceflight experiment and its ground-based analog via 6&deg; head-down tilt bed rest (HDTBR), we show that prolonged microgravity/HDTBR reduces the inversion effect in BM perception. No such change occurs for face perception, highlighting the particular role of gravity in regulating kinematic motion analysis. Moreover, the reduced BM inversion effect is associated with attenuated orientation-dependent neural responses to BM rather than general motion cues and correlated with strengthened functional connectivity between cortical regions dedicated to visual BM processing (i.e., pSTS) and vestibular gravity estimation (i.e., insula). These findings suggest that the neural computation of gravity may act as an embodied constraint, presumably implemented through visuo-vestibular interaction, to sustain the human brain&#39;s selective tuning to life motion signals.</p

Affinity Purification of Angiotensin Converting Enzyme Inhibitory Peptides from Wakame (Undaria Pinnatifida) Using Immobilized ACE on Magnetic Metal Organic Frameworks

Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from marine organism have shown a blood pressure lowering effect with no side effects. A new affinity medium of Fe3O4@ZIF-90 immobilized ACE (Fe3O4@ZIF-90-ACE) was prepared and used in the purification of ACE inhibitory peptides from Wakame (Undaria pinnatifida) protein hydrolysate (&lt;5 kDa). The Fe3O4@ZIF-90 nanoparticles were prepared by a one-pot synthesis and crude ACE extract from pig lung was immobilized onto it, which exhibited excellent stability and reusability. A novel ACE inhibitory peptide, KNFL (inhibitory concentration 50, IC50 = 225.87 μM) was identified by affinity purification using Fe3O4@ZIF-90-ACE combined with reverse phase-high performance liquid chromatography (RP-HPLC) and MALDI-TOF mass spectrometry. Lineweaver–Burk analysis confirmed the non-competitive inhibition pattern of KNFL, and molecular docking showed that it bound at a non-active site of ACE via hydrogen bonds. This demonstrates that affinity purification using Fe3O4@ZIF-90-ACE is a highly efficient method for separating ACE inhibitory peptides from complex protein mixtures and the purified peptide KNFL could be developed as a functional food ingredients against hypertension