bioRxiv Science⌕ Search

Biology subjects

Rummel, A.

Publications and source records attributed to Rummel, A..

2 recordsLinked to original sources

Grip and grasp: lizard claw inspired robotic manipulators

This paper considers the selection of a lizard claw to apply as an end effector on a bioinspired robotic manipulator, to improve grasping efficiency. Our work draws on morphological parameters that influence mechanical grip. By considering geometrical ratios that are built on parameters such as the arm-to-tip angle, the claw inner radius, and the slip distance, our research identifies optimal parameters that influence grip strength and stability. We demonstrate that these parameters, when combined to form two specific indices (the geometric mean, IGM, and the arithmetic mean of deviations, IAMD), provide a basis for more extensive comparisons between the different claw morphologies researched. The claw of Crotaphytus collaris is deduced as being the most suitable candidate for application as a bioinspired end effector in a robotic manipulator used for grasping objects, as it closely aligns with our optimal design criteria. To practically demonstrate gripping and grasping, we use a lightweight ping pong ball as well as larger and heavier objects such as an abalone shell, boxing mitts and a printer spool. Our robotic manipulator integrates dual grasping strategies. These include pinching for delicate objects and scooping for larger, irregular objects, thus enhancing its versatility across different environments and for different applications. Overall, this paper offers valuable new insights into biomimetic manipulator design using claws as end effectors, highlighting the importance of lizard claw selection based on morphology.

bioengineering↗

Synaptotagmin 1 mediates toxicity of botulinum neurotoxin type A

The extreme neurotoxicity of botulinum neurotoxins (BoNTs), broadly used as a therapeutics, is mediated by their direct binding to two plasma membrane receptors: polysialogangliosides (PSGs) and serotype-dependently either synaptotagmin 1/2 (Syt1/2) or synaptic vesicle glycoprotein 2 (SV2). Here, we demonstrate that although BoNT/A serotype binds directly to PSG and SV2, its neurotoxicity depends on Syt1. Using single-molecule superresolution microscopy of pathological concentrations of BoNT/A holotoxins, we demonstrate that the toxin binds to a preassembled PSG-Syt1 complex that forms nanoclusters with SV2 on the plasma membrane of hippocampal neurons. This coincidental interaction controls the selective endocytic targeting of BoNT/A into synaptic vesicles, leading to incapacitation of neuronal communication. Our results suggest that Syt1-SV2 plasma membrane nanoclusters may acts as a common target for various BoNT serotypes. One-Sentence SummaryBoNT/A hijacks an intrinsic tripartite PSG-Syt1-SV2 endocytic sorting mechanism to incapacitate neuronal communication

neuroscience↗