Improving the stability of perovskite quantum dots and adjusting their optical properties are essential for their application in advanced optoelectronic equipment. We provide a simple synthetic method to hybridize perovskite quantum dots and metal-organic frameworks (MOFs) into a polymer matrix. The hybrid material is made by encapsulating perovskite CH3NH3PbBr3 quantum dots in lanthanide-based metal-organic frameworks. A series of lanthanide-based metal-organic frameworks (LnMOFs), namely, [Ln(tpob)(DMF)(H2O)]n (Lntpob, Ln = Nd, Sm, Eu, Gd, Tb, Dy, H3tpob = 1,3,5-tris(4-carbonylphenyloxy)benzene), have been synthesized under solvothermal conditions and fully characterized. Lntpobs display a three-dimensional (3D) pcu network with central-symmetric [Eu2(COO)4] structural building units (SBUs) linked by one-dimensional (1D) chains. CH3NH3PbBr3@Eutpob hybrids were developed through a three-step process, in which the precursor PbBr2@Eutpob was formed by immersing the Eutpob crystal synthesized in the first step into a PbBr2 solution; then the composite materials could form quickly when CH3NH3Br was added to the precursor. Therefore, the hybrid composite material exhibits luminescent properties related to the excitation wavelength in the form of powders or thin films. In addition, the photoluminescence of the CH3NH3PbBr3@Eutpob composite can be improved and maintained for a long time after it is introduced into the poly(methyl methacrylate) (PMMA) matrix. Moreover, the emission peak based on the perovskite quantum dots can still maintain about 85% of the original intensity after being left for 30 days. Also, the obtained PMMA films can achieve tunable emission from red to green.Protein S-palmitoylation is an important post-translational modification (PTM) in blood stages of the malaria parasite, Plasmodium falciparum.  https://www.selleckchem.com/products/Acadesine.html  S-palmitoylation refers to reversible covalent modification of cysteine residues of proteins by saturated fatty acids. In vivo, palmitoylation is regulated by concerted activities of DHHC palmitoyl acyl transferases (DHHC PATs) and acyl protein thioesterases (APTs), which are enzymes responsible for protein palmitoylation and depalmitoylation, respectively. Here, we investigate the role of protein palmitoylation in red blood cell (RBC) invasion by P. falciparum merozoites. We demonstrate for the first time that free merozoites require PAT activity for microneme secretion in response to exposure to the physiologically relevant low [K+] environment, characteristic of blood plasma. We have adapted copper catalyzed alkyne azide chemistry (CuAAC) to image palmitoylation in merozoites and found that exposure to low [K+] activates PAT activity in merozoites. Moreover, using acyl biotin exchange chemistry (ABE) and confocal imaging, we demonstrate that a calcium dependent protein kinase, PfCDPK1, an essential regulator of key invasion processes such as motility and microneme secretion, undergoes dynamic palmitoylation and localizes to the merozoite membrane. Treatment of merozoites with the PAT inhibitor, 2-bromopalmitate (2-BP), effectively inhibits microneme secretion and RBC invasion by the parasite, thus opening the possibility of targeting P. falciparum PATs for antimalarial drug discovery to inhibit blood stage growth of malaria parasites.Biological nanopores are emerging as powerful and low-cost sensors for real-time analysis of biological samples. Proteins can be incorporated inside the nanopore, and ligand binding to the protein adaptor yields changes in nanopore conductance. In order to understand the origin of these conductance changes and develop sensors for detecting metabolites, we tested the signal originating from 13 different protein adaptors. We found that the quality of the protein signal depended on both the size and charge of the protein. The engineering of a dipole within the surface of the adaptor reduced the current noise by slowing the protein dynamics within the nanopore. Further, the charge of the ligand and the induced conformational changes of the adaptor defined the conductance changes upon metabolite binding, suggesting that the protein resides in an electrokinetic minimum within the nanopore, the position of which is altered by the ligand. These results represent an important step toward understanding the dynamics of the electrophoretic trapping of proteins inside nanopores and will allow developing next-generation sensors for metabolome analysis.mRNA-protein interactions play key roles in facilitating various biological functions in gene expression regulations and even the progression of diseases. However, it is still a challenge to directly monitor mRNA-protein interactions in a single living cell at present. Herein, we propose a new strategy for real-time studying of mRNA-protein interactions in a single living cell using fluorescence cross-correlation spectroscopy (FCCS) and molecular beacon (MB) labeling techniques. The c-myc mRNA and coding region determinant binding protein (CRDBP) were used as models. We first evaluated the performances of unmodified (2'-deoxy) and modified (2'-O-methyl) MBs and found that the 2'-O-methyl loop MB (2'-O-methyl loop domain, 2'-deoxy stem region) has high affinity to target mRNA and good nuclease resistance. Then we constructed stable cell line expressing mCherry-CRDBP using lentivirus infection, and on the basis of FCCS, we established an efficient method for quantifying the interaction of c-myc mRNA with CRDBP in a single living cell. The RNA binding domains of CRDBP cover two RNA recognition motifs (RRM) and four K homologies (KH). Furthermore, we constructed the truncated variants and point mutants on RNA binding domains of CRDBP, systematically studied the effects of RNA binding domains of CRDBP on c-myc mRNA-CRDBP interaction in living cells, and found that KH3-4 is indispensable for c-myc mRNA binding, KH1-2 plays a supplementary role, and RRM1-2 shows no binding ability to c-myc mRNA. Our work reveals the mechanisms of c-myc mRNA-CRDBP interactions and provides a general strategy for quantifying the interactions of endogenous mRNA with protein in a single living cell.