A constraint and position identification (CPI) approach for the synthesis of decoupled spatial translational compliant parallel manipulators

This paper introduces a screw theory based method termed constraint and position identification (CPI) approach to synthesize decoupled spatial translational compliant parallel manipulators (XYZ CPMs) with consideration of actuation isolation. The proposed approach is based on a systematic arrangement of rigid stages and compliant modules in a three-legged XYZ CPM system using the constraint spaces and the position spaces of the compliant modules. The constraint spaces and the position spaces are firstly derived based on the screw theory instead of using the rigid-body mechanism design experience. Additionally, the constraint spaces are classified into different constraint combinations, with typical position spaces depicted via geometric entities. Furthermore, the systematic synthesis process based on the constraint combinations and the geometric entities is demonstrated via several examples. Finally, several novel decoupled XYZ CPMs with monolithic configurations are created and verified by finite elements analysis. The present CPI approach enables experts and beginners to synthesize a variety of decoupled XYZ CPMs with consideration of actuation isolation by selecting an appropriate constraint and an optimal position for each of the compliant modules according to a specific application.

Conceptual designs of multi-degree of freedom compliant parallel manipulators composed of wire-beam based compliant mechanisms

This paper proposes conceptual designs of multi-degree(s) of freedom (DOF) compliant parallel manipulators (CPMs) including 3-DOF translational CPMs and 6-DOF CPMs using a building block based pseudo-rigid-body-model (PRBM) approach. The proposed multi-DOF CPMs are composed of wire-beam based compliant mechanisms (WBBCMs) as distributed-compliance compliant building blocks (CBBs). Firstly, a comprehensive literature review for the design approaches of compliant mechanisms is conducted, and a building block based PRBM is then presented, which replaces the traditional kinematic sub-chain with an appropriate multi-DOF CBB. In order to obtain the decoupled 3-DOF translational CPMs (XYZ CPMs), two classes of kinematically decoupled 3-PPPR (P: prismatic joint, R: revolute joint) translational parallel mechanisms (TPMs) and 3-PPPRR TPMs are identified based on the type synthesis of rigid-body parallel mechanisms, and WBBCMs as the associated CBBs are further designed. Via replacing the traditional actuated P joint and the traditional passive PPR/PPRR sub-chain in each leg of the 3-DOF TPM with the counterpart CBBs (i.e. WBBCMs), a number of decoupled XYZ CPMs are obtained by appropriate arrangements. In order to obtain the decoupled 6-DOF CPMs, an orthogonally-arranged decoupled 6-PSS (S: spherical joint) parallel mechanism is first identified, and then two example 6-DOF CPMs are proposed by the building block based PRBM method. It is shown that, among these designs, two types of monolithic XYZ CPM designs with extended life have been presented.

A structure design method for compliant parallel manipulators with actuation isolation

Since precise linear actuators of a compliant parallel manipulator suffer from their inability to tolerate the transverse motion/load in the multi-axis motion, actuation isolation should be considered in the compliant manipulator design to eliminate the transverse motion at the point of actuation. This paper presents an effective design method for constructing compliant parallel manipulators with actuation isolation, by adding the same number of actuation legs as the number of the DOF (degree of freedom) of the original mechanism. The method is demonstrated by two design case studies, one of which is quantitatively studied by analytical modelling. The modelling results confirm possible inherent issues of the proposed structure design method such as increased primary stiffness, introduced extra parasitic motions and cross-axis coupling motions.

A novel activation mechanism for Clostridial bacteriophage endolysins

Bacteriophage-encoded endolysins are produced at the end of the phage lytic cycle for the degradation of the host bacterial cell. Endolysins offer the potential as alternatives to antibiotics as biocontrol agents or therapeutics. The lytic mechanisms of three bacteriophage endolysins that target Clostridium species living under different conditions were investigated. For these endolysins a trigger and release mechanism is proposed for their activation. During host lysis, holin lesion formation suddenly permeabilises the membrane which exposes the cytosol-sequestered endolysins to a sudden environmental shock. This shock is suggested to trigger a conformational switch of the endolysins between two distinct dimer states. The switch between dimer states is proposed to activate a novel autocleavage mechanism that cleaves the linker connecting the N-terminal catalytic domain and the C-terminal domain to release the catalytic domain for more efficient digestion of the bacterial cell wall. Crystal structures of cleaved fragments of CD27L and CTP1L were previously obtained. In these structures cleavage occurs at the stem of the linker connected to the C-terminal domain. Despite a sequence identity of only 22% between 81 residues of the C-terminal domains of CD27L and CTP1L, they represent a novel fold that is identified in a number of different lysins. Within the crystal structures the two distinct dimerization modes are represented: the elongated head‐on dimer and the side-by‐side dimer. Introducing mutations that inhibit either of the dimerization states caused a decrease in the efficiency of both the autocleavage mechanism and the lytic activity of the endolysins. The two dimer states were validated for the full-length endolysins in solution by using right angle light scattering, small angle X‐ray scattering and cross-linking experiments. Overall, the data represents a new type of regulation governed by the C-terminal domains that is used to activate these endolysins once they enter the bacterial cell wall.