Multi-Material Topology Optimization of Structures Using an Ordered Ersatz Material Model

This paper proposes a new element-based multi-material topology optimization algorithm using a single variable for minimizing compliance subject to a mass constraint.A single variable based on the normalized elemental density is used to overcome the occurrence of meaningless design variables and save computational cost.Different from the traditional material penalization scheme,the algorithm is established on the ordered ersatz material model,which linearly interpolates Young’s modulus for relaxed design variables.To achieve a multi-material design,the multiple floating projection constraints are adopted to gradually push elemental design variables to multiple discrete values.For the convergent element-based solution,the multiple level-set functions are constructed to tentatively extract the smooth interface between two adjacent materials.Some 2D and 3D numerical examples are presented to demonstrate the effectiveness of the proposed algorithm and the possible advantage of the multi-material designs over the traditional solid-void designs.

Synchronization of two 3-scroll hyperchaotic attractors using wavelet transform

The synchronization of two 3-scroll hyperchaotie attractors is realized based on wavelet transform and single variables＇ feedstock. In the transmitter, one signal is decomposed by wavelet transform and the detailed information is removed, then the component with low frequency is reconstructed and sent into the channel In the receiver, the received signal is used as the feedback signal to realize the synchronization of two chaotic systems. Using this synchronous method, the transmitting signal is transported in compressible way, the system resource is saved, furthermore, because the transported signal is not a whole chaotic signal, the performance of security of the system is improved.

Screening of scFvs against cTnI from Phage Display Antibody Library and Their Expression in E.coli Rosetta

The single chain variable fragments of antibodies(scFvs) against cTnI were screened from the phage display antibody library by using cTnI as the target antigen. After four rounds of panning, four clones(H2, G5, A9, B9) from the phage display antibody library were verified to show higher binding affinity for cTnI by ELISA and to contain the variable region genes of the light and heavy chains of scFvs by sequencing. The variable region genes of scFvs H2 and G5 were successfully amplified by polymerase chain reactions(PCR) and cloned into expression vector pPELB and expressed as a soluble protein in E.coli Rosetta, whose expression yield was about 2% of total proteins. The expressed proteins were purified by nickel(Ni) affinity chromatography and a single band is shown in the position of 28 kDa on SDS-PAGE. The western blot analysis result verifies that the expressed scFv proteins are capable of binding with monoclonal antibodies against hexa-histidine, indicating that they are hexa-histidin-tagged aim proteins. The immunoassay demonstrates that the expressed scFv proteins are able to specifically react with cTnI molecules. The association constant(K_A) values range from 1.2×10 4 to 1.7 ×10 5 L/mol that are correspondent to the affinities of polyclonal antibodies against cTnI from rabbits. These antibodies can be valuable reagents for the immunoassay of cTnI.

Engineering a cell-penetrating hyperstable antibody scFv(Ras)-An extraordinary approach to cancer therapeutics

In the modern pharmaceutical industry,monoclonal antibodies are often used as therapeutic agents.However,they are restricted to cell surface antigens due to their inability to penetrate the outer cell membrane and maintain normal function in the reducing environment.Additionally,it can lead to cytotoxicity since it attacks cancerous cells by mimicking the human immune system.As an alternative,this study modifies the hyperstable single-chain fragment variable(scFv)antibody to eliminate cancer using its linear shape.The scFv(F8)antibody model was modified to recognize human Ras protein by altering residues in the antigen-binding site.Furthermore,a cell-penetrating peptide(CPP)was attached to the scFv(Ras)antibody model to allow entrance to the cell,creating CPP-scFv(Ras).Sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE),western blotting,and the binding assay were performed to prove its effectiveness.As a result,CPP-scFv(Ras)was successfully engineered and bound to the antigen,HRas(G12V).