ND Biosciences

Description

ND Biosciences is a spinoff from the Swiss Federal Institute of Technology in Lausanne (EPFL), dedicated to developing next-generation therapeutics for neurodegenerative diseases (NDs) such as Parkinson's and Alzheimer's Disease. Leveraging over 15 years of research, ND Biosciences has created an integrated suite of novel, validated, and patented drug-discovery platforms. These platforms accurately replicate the diversity, structural, and biochemical properties of pathogenic protein aggregates observed in patient brains, enabling more precise antigen generation for drug development. By utilizing cellular models that mimic different stages of protein aggregation, including early and terminal stages leading to neurodegeneration, ND Biosciences can assess efficacy and identify next-generation hits using translationally-relevant models.

Official source

https://nd-biosciences.com

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Neurodegenerative disease

A neurodegenerative disease is caused by the progressive loss of structure or function of neurons, in the process known as neurodegeneration. Such neuronal damage may ultimately involve cell death. Neurodegenerative diseases include amyotrophic lateral sclerosis, multiple sclerosis, Parkinson's disease, Alzheimer's disease, Huntington's disease, multiple system atrophy, and prion diseases. Neurodegeneration can be found in the brain at many different levels of neuronal circuitry, ranging from molecular to systemic.

Protein aggregation

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state.

Prion

A prion ˈpriːɒn is a misfolded protein that can transmit its misfoldedness to normal variants of the same protein and trigger cellular death. Prions cause prion diseases known as transmissible spongiform encephalopathies (TSEs) that are transmissible, fatal neurodegenerative diseases in humans and animals. The proteins may misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein. The consequent abnormal three-dimensional structure confers on them the ability to cause misfolding of other proteins.

Amyloid

Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

ND Biosciences

Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization.

Method of preparation of amyloidogenic protein aggregates and uses thereof

Deconstructing and Reconstructing the Complexity of Tau pathology

Deconstructing and Reconstructing the Complexity of Tau pathology

Method of preparation of amyloidogenic protein aggregates and uses thereof

Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization.