Francesco Simone Ruggeri

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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 devia ...

Cells are extremely complex systems able to modify actively their metabolism and behaviour in response to environmental conditions and stimuli, such as pathogenic agents or drugs. The comprehension of these responses is central to understand the molecular ...

Background: A wide class of human diseases and neurodegenerative disorders, such as Alzheimer's disease, is due to the failure of a specific peptide or protein to keep its native functional conformational state and to undergo a conformational change into a ...

Droplet microfluidics has emerged as a powerful platform allowing a large number of individual reactions to be carried out in spatially distinct microcompartments. Due to their small size, however, the spectroscopic characterisation of species encapsulated ...

Converging evidence points to the N-terminal domain comprising the first 17 amino acids of the Huntingtin protein (Nt17) as a key regulator of its aggregation, cellular properties and toxicity. In this study, we further investigated the interplay between N ...

Protein nanofibrils were first discovered in the context of misfolding and neurodegenerative diseases but have recently been found in naturally occurring functional materials including algal adhesives, bacterial coatings, and even mammalian melanosomes. Th ...

The existence of life in extreme conditions, in particular in extraterrestrial environments, is certainly one of the most intriguing scientific questions of our time. In this report, we demonstrate the use of an innovative nanoscale motion sensor in life-s ...

Today, more than 40 million people worldwide are affected by neurodegenerative disorders. Onset of these diseases is associated with insoluble fibrillar protein aggregates, termed amyloids. The molecular origin and the link between amyloid formation and di ...

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 ...

The natural enzymes involved in regulating many of the posttranslational modifications (PTMs) within the first 17 residues (Nt17) of Huntingtin exon1 (Httex1) remain unknown. A semisynthetic strategy that allows the site-specific introduction of PTMs withi ...

A wide consensus based on robust experimental evidence indicates pyroglutamylated amyloid-beta isoform (A beta pE3-42) as one of the most neurotoxic peptides involved in the onset of Alzheimer's disease. Furthermore, A beta pE3-42 co-oligomerized with exce ...

Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josep ...

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 cha ...

Over the last two decades, the identification of missense mutations in the alpha-synuclein (alpha-Syn) gene SNCA in families with inherited Parkinson disease (PD) has reinforced the central role of alpha-Syn in PD pathogenesis. Recently, a new missense mut ...

We have synthesized a 17-mer peptide (ER17p) that is issued from the hinge region of the estrogen receptor and which activates the proliferation of breast carcinoma cells in steroid-deprived conditions. In the present paper, we show that at a concentration ...

The presence of expanded poly-glutamine (polyQ) repeats in proteins is directly linked to the pathogenesis of several neurodegenerative diseases, including Huntington's disease. However, the molecular and structural basis underlying the increased toxicity ...

Francesco Simone Ruggeri

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Identification of Oxidative Stress in Red Blood Cells with Nanoscale Chemical Resolution by Infrared Nanospectroscopy

Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection

AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species

Nanoscale spatially resolved infrared spectra from single microdroplets

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1

Micro- and nanoscale hierarchical structure of core-shell protein microgels

Detecting nanoscale vibrations as signature of life

New Insights Into Amyloid Formation and Structure by Innovative Atomic Force Microscopy Methods

Infrared nanospectroscopic mapping of a single metaphase chromosome

One-Pot Semisynthesis of Exon 1 of the Huntingtin Protein: New Tools for Elucidating the Role of Posttranslational Modifications in the Pathogenesis of Huntington's Disease

A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates

Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

Hierarchical Protofilament Intertwining Rules the Formation of Mixed‐Curvature Amyloid Polymorphs

The H50Q Mutation Enhances alpha-Synuclein Aggregation, Secretion, and Toxicity

Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor alpha-derived peptide

Nanoscale studies link amyloid maturity with polyglutamine diseases onset

Identification and nanomechanical characterization of the fundamental single-strand protofilaments of amyloid α-synuclein fibrils