The ability to control the dimensions and properties of nanomaterials is fundamental to the creation of new functions and improvement of their performances in the applications of interest. Herein, we report a strategy based on glucan multivalent interactions for the simultaneous exfoliation and functionalization of two-dimensional transition metal dichalcogenides (TMDs) in an aqueous solution. The multivalent hydrogen bonding of dextran with bulk TMDs (WS2, WSe2, and MoSe2) in liquid exfoliation effectively produces TMD monolayers with binding multivalency for pathogenic bacteria. Density functional theory simulation reveals that the multivalent hydrogen bonding between dextran and TMD monolayers is very strong and thermodynamically favored (ΔEb = −0.52 eV). The resulting dextran/TMD hybrids (dex-TMDs) exhibit a stronger affinity (Kd = 11 nM) to Escherichia coli O157:H7 (E. coli) than E. coli-specific antibodies and aptamers. The dex-TMDs can effectively detect a single copy of E. coli based on their Raman signal.
It is very challenging to accurately quantify the amounts of amyloid peptides Aβ40 and Aβ42, which are Alzheimer's disease (AD) biomarkers, in blood owing to their low levels. This has driven the development of sensitive and noninvasive sensing methods for the early diagnosis of AD. Here, an approach for the synthesis of Ag nanogap shells (AgNGSs) is reported as surface‐enhanced Raman scattering (SERS) colloidal nanoprobes for the sensitive, selective, and multiplexed detection of Aβ40 and Aβ42 in blood. Raman label chemicals used for SERS signal generation modulate the reaction rate for AgNGSs production through the formation of an Ag‐thiolate lamella structure, enabling the control of nanogaps at one nanometer resolution. The AgNGSs embedded with the Raman label chemicals emit their unique SERS signals with a huge intensity enhancement of up to 107 and long‐term stability. The AgNGS nanoprobes, conjugated with an antibody specific to Aβ40 or Aβ42, are able to detect these AD biomarkers in a multiplexed manner in human serum based on the AgNGS SERS signals. Detection is possible for amounts as low as 0.25 pg mL−1. The AgNGS nanoprobe‐based sandwich assay has a detection dynamic range two orders of magnitude wider than that of a conventional enzyme‐linked immunosorbent assay.
It is not facile to obtain ultrathin two-dimensional (2D) WO 3 nanosheets through the exfoliation of their bulk counterpart in solution due to strong covalent interaction between interlayers. In addition, they require additional functionalization with cocatalysts to expand their applicability in photocatalytic organic reactions owing to their insufficient conduction band edge position. Here, we report a chemical approach for the simultaneous production and functionalization of ultrathin 2D WO 3 nanosheets through the direct conversion of metallic WS 2 nanosheets, accomplished by the spontaneous formation and deposition of PdO nanoclusters on the nanosheet surface in H 2 O. When chemically exfoliated metallic WS 2 nanosheets were simply mixed with K 2 PdCl 4 in H 2 O under mild conditions (50 °C, 1 h), they were converted to semiconducting WO 3 nanosheets on which PdO nanoclusters of a uniform size (∼3 nm) were spontaneously formed, leading to the production of PdO-functionalized ultrathin WO 3 (PdO@WO 3 ) nanohybrids. The conversion yield of WO 3 nanosheets from metallic WS 2 nanosheets increased with increasing coverage of PdO nanoclusters on the nanosheet surface. In addition, the conversion of WO 3 nanosheets induced by PdO nanocluster formation was effective only in H 2 O but not in organic solvents, such as N-methylpyrrolidone and acetonitrile. A mechanical study suggests that the chemisorption of hydrated Pd precursors on the chalcogens of metallic WS 2 nanosheets leads to their facile oxidation by water molecules, producing WO 3 nanosheets covered with PdO nanoclusters. The as-prepared PdO@WO 3 nanosheets exhibited excellent photocatalytic activity and recyclability in Suzuki cross-coupling reactions of various aryl halides under visible light irradiation.
The regulation of tyrosinase activity and reactive oxygen species is of great importance for the prevention of dermatological disorders in the fields of medicine and cosmetics. Herein, we report a strategy based on solid-phase peptide chemistry for the synthesis of β-lactoglobulin peptide fragment/caffeic acid (CA) conjugates (CA-Peps) with dual activities of tyrosinase inhibition and antioxidation. The purity of the prepared conjugates, CA-MHIR, CA-HIRL, and CA-HIR, significantly increased to 99%, as acetonide-protected CA was employed in solid-phase coupling reactions on Rink amide resins. The tyrosinase inhibitory activities of all CA-Pep derivatives were higher than the activity of kojic acid, and CA-MHIR exhibited the highest tyrosinase inhibition activity (IC = 47.9 μM). Moreover, CA-Pep derivatives displayed significantly enhanced antioxidant activities in the peroxidation of linoleic acid as compared to the pristine peptide fragments. All CA-Pep derivatives showed no cytotoxicity against B16-F1 melanoma cells.
Antibodies are widely used as recognition elements in sensing and therapy, but they suffer from poor stability, long discovery time, and high cost. Herein, a facile approach to create antibody mimics with flexible recognition phases and luminescent rigid scaffolds for the selective recognition, detection, and inactivation of pathogenic bacteria is reported. Tripeptides with a nitriloacetate‐Cu group are spontaneously assembled on transition metal dichalcogenide (TMD) nanosheets via coordination bonding, providing a diversity of TMD‐tripeptide assembly (TPA) antibody mimics. TMD‐TPA antibody mimics can selectively recognize various pathogenic bacteria with nanomolar affinities. The bacterial binding sites for TMD‐TPA are identified by experiments and molecular dynamics simulations, revealing that the dynamic and multivalent interactions of artificial antibodies play a crucial role for their recognition selectivity and affinity. The artificial antibodies allow the rapid and selective detection of pathogenic bacteria at single copy in human serum and urine, and their effective inactivation for therapy of infected mice. This work demonstrates the potential of TMD‐TPA antibody mimics as an alternative to natural antibodies for sensing and therapy.
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