The electronic local density of states (LDOS) of single PbSe quantum dots (QDs) and QD molecules is explored using low-temperature scanning tunneling microscopy (STM) and spectroscopy (STS). Both individual PbSe QDs and molecular aggregates of PbSe QDs (dimers, trimers, etc.) are mechanically stabilized in a two-dimensional superlattice of wide band gap CdSe QDs acting as an inert matrix. The LDOS measured at individual QDs dispersed in the matrix is identical to that of single isolated QDs chemically linked to a substrate. We investigate the degree of quantum mechanical coupling between the PbSe QDs in molecular aggregates by comparing the LDOS measured at each site in the aggregates to that of an individual PbSe QD. We observe a variable broadening of the resonances indicating a spatially dependent degree of electron delocalization in the molecular aggregates.
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http://dx.doi.org/10.1021/nn7003876 | DOI Listing |
Am J Kidney Dis
December 2024
Service de Néphrologie, Hémodialyse et Transplantation Rénale, Centre de référence MARHEA, CHRU Brest, Brest, France; Institut de Recherche Expérimentale et Clinique (IREC), UCLouvain, Brussels, Belgium. Electronic address:
Rationale & Objective: Monoallelic predicted Loss-of-Function (pLoF) variants in IFT140 have recently been associated with an autosomal dominant polycystic kidney disease (ADPKD)-like phenotype. This study sought to enhance the characterization of this phenotype.
Study Design: Case series.
Int J Biol Macromol
December 2024
Institute for Complex Systems, National Research Council, Piazzale Aldo Moro 5, 00185 Rome, Italy; Department of Physics, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy. Electronic address:
Polyelectrolyte complexes (PECs), formed via the self-assembly of oppositely charged polysaccharides, are highly valued for their biocompatibility, biodegradability, and hydrophilicity, offering significant potential for biotechnological applications. However, the complex nature and lack of insight at a molecular level into polyelectrolytes conformation and aggregation often hinders the possibility of achieving an optimal control of PEC systems, limiting their practical applications. To address this problem, an in-depth investigation of PECs microscopic structural organization is required.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 2024
Department of Chemical Engineering, Osaka Metropolitan University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka, 599-8531, Japan. Electronic address:
Acyl-acyl carrier protein (acyl-ACP) reductase (AAR) is a crucial enzyme in alka(e)ne production by recombinant Escherichia coli (E. coli). Engineered AAR expressed in E.
View Article and Find Full Text PDFEur J Med Chem
December 2024
Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Sinai University, Kantara Branch, Ismailia, 41636, Egypt.
Alzheimer's disease (AD) is primarily caused by oxidative stress, hyperphosphorylated τ-protein aggregation, and amyloid-β deposition. Changes in dopaminergic and serotoninergic neurotransmitter pathways are linked to certain symptoms of AD. Derivatives of bicyclic and tricyclic cyclohepta[b]thiophene were developed to identify new potential candidates as acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors for the treatment of AD.
View Article and Find Full Text PDFJ Biomol Struct Dyn
December 2024
Centre for Biotechnology, Siksha 'O' Anusandhan (Deemed to Be University), Bhubaneswar, Odisha, India.
In the relentless pursuit of unraveling the intricate pathophysiology of Alzheimer's disease (AD), amyloid β (Aβ) proteins emerge as focal points due to their pivotal role in disease progression. The pathological hallmark of AD involves the aberrant aggregation of Aβ peptides into amyloid fibrils, precipitating a cascade of neurodegenerative events culminating in cognitive decline and neuronal loss. This study adopts a computational framework to investigate the potential therapeutic efficacy of novel biosurfactants (BS) in mitigating Aβ fibril formation.
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