Rapid and effective differentiation and killing of microbial pathogens are major challenges in the diagnosis and treatment of infectious diseases. Here, we report a novel system based on the conjugated polymer poly[(9,9-bis{6′-[N-(triethylene glycol methyl ether)-di(1H-imidazolium)methane]hexyl}-2,7-fluorene)-co-4,7-di-2-thienyl-2,1,3-benzothiadiazole] tetrabromide (PFDBT-BIMEG), which enables efficient microbial pathogen discrimination and killing. The functional side chains of PFDBT-BIMEG enabled both electrostatic and salt bridge interactions with microorganisms. Microorganism binding events caused a change in the aggregation structure of PFDBT-BIMEG, which could be recognized by a change of its fluorescence signal by intramolecular Forster resonance energy transfer (FRET). This sensing strategy allowed rapid and sensitive distinction of microbial pathogens within 15 min. We performed linear discrimination analysis that featured this advance to confirm that the polymer PFDBT-BIMEG could accurately classify microbial pathogens. Owing to the different adhesion mechanism of PFDBT-BIMEG to the surface of the microorganisms, we applied different sterilization strategies for each kind of microbial pathogen. The microbial pathogens could be efficiently killed by reactive oxygen species produced from PFDBT-BIMEG under irradiation, avoiding the use of any other antibacterial agents. This methodology, which combines pathogen discrimination and killing, represents a promising alternative to current diagnostic platforms.

Protein misfolding and aberrant aggregations are associated with multiple prevalent and intractable diseases. Inhibition of amyloid assembly is apromising strategy for the treatment of amyloidosis.R eported here is the design and synthesis of areactive conjugated polymer,apoly(p-phenylene vinylene) derivative,f unctionalizedw ith p-nitrophenyl esters (PPV-NP) and it inhibits the assembly of amyloid proteins, degrades preformed fibrils,a nd reduces the cytotoxicity of amyloid aggregations in living cells.PPV-NP is attached to the proteins through hydrophobic interactions and irreversible covalent linkage.P PV-NP also exhibited the capacity to eliminate Ab plaques in brain slices in ex vivo assays.T his work represents an innovative attempt to inhibit protein pathogenic aggregates,and may offer insights into the development of therapeutic strategies for amyloidosis.Proteins are one of the most important basic bio-macromolecules in organisms.T he aberrant assembly of proteins into insoluble amyloid aggregates would disrupt their biological functions and result in the generation of toxic intermediates and amyloidosis,w hich are relevant to ar ange of intractable human disorders such as Alzheimersd isease, Parkinsonsd isease,d ialysis-related amyloidosis,a nd type-2 diabetes. [1][2][3][4][5][6][7] On this account, numerous approaches to inhibit amyloid assembly have emerged, ranging from synthetic and natural small-molecule compounds, [4,8,9] peptides, [10,11] antibodies, [12] and nanoparticles [13,14] to artificial chaperones, [15] which make certain achievements to the inhibition of pathogenic aggregates.H owever,t od ate,t he pharmacological treatments for these diseases are still unsatisfactory. [16] Rational chemical designs to effectively inhibit and disrupt the amyloid assembly are still of great significance.In fact, most previous inhibitors functioned through noncovalent interactions,s uch as hydrophobic interactions, p-p stacking,e lectrostatic interactions,a nd hydrogen bonding. These interactions are intrinsically weak and susceptible to the surrounding environment. [17] Thef luctuation of either pH or temperature may induce the disassembly of inhibitor/ protein complexes,and would make the inhibitors invalid. In contrast, covalent interactions are more chemically stable and not susceptible to the fluctuation of surrounding environment. Reactions between inhibitors and proteins are usually irreversible,and inhibitors could remain attached to proteins for long time.T hus,d eveloping new inhibiting materials for amyloid assembly with acovalent-linking strategy is expected to lead to prolonged duration of inhibition and improved efficiency.T he amphiphilic conjugated polymers are considered pioneering materials in the biomedical field owing to their unique photoelectrical properties. [18][19][20][21][22][23][24] Here,w e designed and synthesized ar eactive conjugated polymer, ap oly(p-phenylene vinylene) derivative,f unctionalized with p-nitrophenyl active esters (PPV-NP) to inhibit protein assembly and disru...