Publications by authors named "Giovanni Dietler"

Amyloid polymorphism is a hallmark of almost all amyloid species, yet the mechanisms underlying the formation of amyloid polymorphs and their complex architectures remain elusive. Commonly, two main mesoscopic topologies are found in amyloid polymorphs characterized by non-zero Gaussian and mean curvatures: twisted ribbons and helical fibrils, respectively. Here, a rich heterogeneity of configurations is demonstrated on insulin amyloid fibrils, where protofilament packing can occur, besides the common polymorphs, also in a combined mode forming mixed-curvature polymorphs.

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The emergence of antibiotic and antifungal resistant microorganisms represents nowadays a major public health issue that might push humanity into a post-antibiotic/antifungal era. One of the approaches to avoid such a catastrophe is to advance rapid antibiotic and antifungal susceptibility tests. In this study, we present a compact, optical fiber-based nanomotion sensor to achieve this goal by monitoring the dynamic nanoscale oscillation of a cantilever related to microorganism viability.

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Article Synopsis
  • The N-terminal domain (Nt17) of the Huntingtin protein is crucial for regulating its aggregation and toxicity, particularly in relation to the length of the polyQ repeat.
  • Removing or altering Nt17 affects Httex1's aggregation, reduces cell inclusions, enhances neuronal uptake, and can prevent cell death in models of Huntington's disease.
  • The findings suggest that Nt17 is a central regulator in the behavior of Httex1, making it a potential target for therapies aimed at reducing Huntingtin-related neurotoxicity.
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Atomic force microscopy (AFM)-based nanomotion detection is a label-free technique that has been used to monitor the response of microorganisms to antibiotics in a time frame of minutes. The method consists of attaching living organisms onto an AFM cantilever and in monitoring its nanometric scale oscillations as a function of different physical-chemical stimuli. Up to now, we only used the cantilever oscillations variance signal to assess the viability of the attached organisms.

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The phenomenon of amyloid polymorphism is a key feature of protein aggregation. Unravelling this phenomenon is of great significance for understanding the underlying molecular mechanisms associated with neurodegenerative diseases and for the development of amyloid-based functional biomaterials. However, the understanding of the molecular origins and the physicochemical factors modulating amyloid polymorphs remains challenging.

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Living single yeast cells show a specific cellular motion at the nanometer scale with a magnitude that is proportional to the cellular activity of the cell. We characterized this cellular nanomotion pattern of nonattached single yeast cells using classical optical microscopy. The distribution of the cellular displacements over a short time period is distinct from random motion.

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Hydrogen as an antioxidant gas has been widely used in the medical and biological fields for preventing cancer or treating inflammation. However, controlling the hydrogen concentration is crucial for practical use due to its explosive property when its volume concentration in air reaches the explosive limit (4%). In this work, a polymer-based microcantilever (μ-cantilever) hydrogen sensor located at the end of a fiber tip is proposed to detect the hydrogen concentration in medical and biological applications.

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By a micro-experimental methodology, we study the ongoing molecular process inside coarse fibrin networks by means of microrheology. We made these networks gelate around a probe microbead, allowing us to observe a temporal evolution compatible with the well-known molecular formation of fibrin networks in four steps: monomer, protofibril, fiber and network. Thanks to the access that optical-trapping interferometry provides to the short-time scale on the bead's Brownian motion, we observe a Kelvin-Voigt mechanical behavior from low to high frequencies, range not available in conventional rheometry.

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The insurgence of newly arising, rapidly developing health threats, such as drug-resistant bacteria and cancers, is one of the most urgent public-health issues of modern times. This menace calls for the development of sensitive and reliable diagnostic tools to monitor the response of single cells to chemical or pharmaceutical stimuli. Recently, it has been demonstrated that all living organisms oscillate at a nanometric scale and that these oscillations stop as soon as the organisms die.

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The formation of amyloid fibrils is a characterizing feature of a range of protein misfolding diseases, including Parkinson's disease. The propensity of native proteins to form such amyloid fibril, both and , is highly sensitive to the surrounding environment, which can alter the aggregation kinetics and fibrillization mechanisms. Here, we investigate systematically the influence of several representative environmental stimuli on α-synuclein aggregation, including hydrodynamic mixing, the presence of an air-water interface and sedimentation.

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A current-driven source of long-range surface plasmons (LRSPs) on a duplex metal nanolayer is reported. Electrical excitation of LRSPs was experimentally observed in a planar structure, where an organic light-emitting film was sandwiched between two metal nanolayers that served as electrodes. To achieve the LRSP propagation in these metal nanolayers at the interface with air, the light-emitting structure was bordered by a one-dimensional photonic crystal (PC) on the other side.

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In bacteria, nucleoid associated proteins (NAPs) take part in active chromosome organization by supercoil management, three-dimensional DNA looping and direct transcriptional control. Mycobacterial integration host factor (mIHF, rv1388) is a NAP restricted to Actinobacteria and essential for survival of the human pathogen Mycobacterium tuberculosis. We show in vitro that DNA binding by mIHF strongly stabilizes the protein and increases its melting temperature.

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The xanthophyll cycle is a regulatory mechanism operating in the photosynthetic apparatus of plants. It consists of the conversion of the xanthophyll pigment violaxanthin to zeaxanthin, and vice versa, in response to light intensity. According to the current understanding, one of the modes of regulatory activity of the cycle is associated with the influence on a molecular organization of pigment-protein complexes.

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Chemical characterization at the nanoscale is of significant importance for many applications in physics, analytical chemistry, material science, and biology. Despite the intensive studies in the infrared range, high-spatial-resolution and high-sensitivity imaging for compositional identification in the visible range is rarely exploited. In this work, we present a gap-plasmon-enhanced imaging approach based on photothermal-induced resonance (PTIR) for nanoscale chemical identification.

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The integrity of the chromatin structure is essential to every process occurring within eukaryotic nuclei. However, there are no reliable tools to decipher the molecular composition of metaphase chromosomes. Here, we have applied infrared nanospectroscopy (AFM-IR) to demonstrate molecular difference between eu- and heterochromatin and generate infrared maps of single metaphase chromosomes revealing detailed information on their molecular composition, with nanometric lateral spatial resolution.

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Here, a soft robotic microgripper is presented that consists of a smart actuated microgel connected to a spatially photopatterned multifunctional base. When pressed onto a target object, the microgel component conforms to its shape, thus providing a simple and adaptive solution for versatile micromanipulation. Without the need for active visual or force feedback, objects of widely varying mechanical and surface properties are reliably gripped through a combination of geometrical interlocking mechanisms instantiated by reversible shape-memory and thermal responsive swelling of the microgel.

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We study the dynamics of knotted deformable closed chains sedimenting in a viscous fluid. We show experimentally that trefoil and other torus knots often attain a remarkably regular horizontal toroidal structure while sedimenting, with a number of intertwined loops, oscillating periodically around each other. We then recover this motion numerically and find out that it is accompanied by a very slow rotation around the vertical symmetry axis.

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During their lifespan, Red blood cells (RBC), due to their inability to self-replicate, undergo an ageing degradation phenomenon. This pathway, both in vitro and in vivo, consists of a series of chemical and morphological modifications, which include deviation from the biconcave cellular shape, oxidative stress, membrane peroxidation, lipid content decrease and uncoupling of the membrane-skeleton from the lipid bilayer. Here, we use the capabilities of atomic force microscopy based infrared nanospectroscopy (AFM-IR) to study and correlate, with nanoscale resolution, the morphological and chemical modifications that occur during the natural degradation of RBCs at the subcellular level.

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Article Synopsis
  • Huntington's disease is caused by a genetic mutation leading to the toxic accumulation of the Huntingtin protein, and phosphorylation of this protein is crucial for its behavior and effects in cells.
  • Phosphorylation at specific residues (Ser-13 and Ser-16) has significant effects on reducing the aggregation of mutant protein, while also disrupting critical structural features, unlike phosphomimetic substitutions which do not fully replicate these effects.
  • Understanding these phosphorylation processes sheds light on the potential for targeting the enzymes involved as therapeutic strategies for managing Huntington's disease.
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Plasmonic nanoantennas offer new applications in mid-infrared (mid-IR) absorption spectroscopy with ultrasensitive detection of structural signatures of biomolecules, such as proteins, due to their strong resonant near-fields. The amide I fingerprint of a protein contains conformational information that is greatly important for understanding its function in health and disease. Here, we introduce a non-invasive, label-free mid-IR nanoantenna-array sensor for secondary structure identification of nanometer-thin protein layers in aqueous solution by resolving the content of plasmonically enhanced amide I signatures.

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The formation and spreading of amyloid aggregates from the presynaptic protein α-synuclein in the brain play central roles in the pathogenesis of Parkinson's disease. Here, we use high-resolution atomic force microscopy to investigate the early oligomerization events of α-synuclein with single monomer angstrom resolution. We identify, visualize, and characterize directly the smallest elementary unit in the hierarchical assembly of amyloid fibrils, termed here single-strand protofilaments.

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Exposure to ionizing radiation can induce cellular defense mechanisms including cell activation and rapid proliferation prior to metastasis and in extreme cases can result in cell death. Herewith we apply infrared nano- and microspectroscopy combined with multidimensional data analysis to characterize the effect of ionizing radiation on single glioblastoma nuclei isolated from cells treated with 10 Gy of X-rays or 1 and 10 Gy of protons. We observed chromatin fragmentation related to the formation of apoptotic bodies following X-ray exposure.

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A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.

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Infectious diseases are caused by pathogenic microorganisms and are often severe. Time to fully characterize an infectious agent after sampling and to find the right antibiotic and dose are important factors in the overall success of a patient's treatment. Previous results suggest that a nanomotion detection method could be a convenient tool for reducing antibiotic sensitivity characterization time to several hours.

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Cells are extremely complex systems able to actively modify their metabolism and behavior in response to environmental conditions and stimuli such as pathogenic agents or drugs. The comprehension of these responses is central to understand the molecular bases of human pathologies, including amyloid misfolding diseases. Conventional bulk biological assays are limited by intrinsic cellular heterogeneity in gene, protein and metabolite expression, and can investigate only indirectly cellular reactions in non-physiological conditions.

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