Kerensa Broersen

ORCID: 0000-0002-9596-0607
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About
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Research Areas
  • Alzheimer's disease research and treatments
  • Proteins in Food Systems
  • 3D Printing in Biomedical Research
  • Protein Structure and Dynamics
  • Computational Drug Discovery Methods
  • Cholinesterase and Neurodegenerative Diseases
  • Supramolecular Self-Assembly in Materials
  • Parkinson's Disease Mechanisms and Treatments
  • Mitochondrial Function and Pathology
  • Probiotics and Fermented Foods
  • Enzyme Production and Characterization
  • Enzyme Structure and Function
  • Machine Learning in Bioinformatics
  • Pluripotent Stem Cells Research
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Biochemical effects in animals
  • Advanced Glycation End Products research
  • Barrier Structure and Function Studies
  • Protein purification and stability
  • Drug Transport and Resistance Mechanisms
  • Protein Hydrolysis and Bioactive Peptides
  • Planarian Biology and Electrostimulation
  • Biochemical Acid Research Studies
  • Cellular transport and secretion
  • Neuroscience and Neural Engineering

University of Twente
2015-2024

Nederlands Instituut Voor Zuivel Oonderzoek
2024

Nederlandse Spoorwegen
2022

VIB-KU Leuven Center for Brain & Disease Research
2012-2019

Stem Cell Technology (Taiwan)
2019

Vlaams Instituut voor Biotechnologie
2010-2012

Vrije Universiteit Brussel
2010-2012

KU Leuven
2012

Switch
2009

Wageningen University & Research
2003-2008

Since the reformulation of amyloid cascade hypothesis to focus on oligomeric aggregates beta as prime toxic species causing Alzheimer's disease, many researchers refocused detecting a specific molecular assembly defined size thatis main trigger disease. The result has been identification host assemblies containing from two up hundred molecules peptide, which were all found impair memory formation in mice. This clearly demonstrates that is insufficient define toxicity and peptide conformation...

10.1186/alzrt36 article EN cc-by Alzheimer s Research & Therapy 2010-01-01

We provide a validated and rapid protocol for the solubilization of amyloid β-peptide (Aβ). This procedure involves sequential using structure-breaking organic solvents hexafluoroisopropanol DMSO followed by column purification. The low solubility tendency Aβ to aggregate considerably impede in vitro handling biophysical or biological investigation Aβ, despite interest this peptide because its implication Alzheimer's disease. main advantage proposed over others is that it results...

10.1093/protein/gzr020 article EN Protein Engineering Design and Selection 2011-05-11

Research Article15 April 2011Open Access Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β′-site increases Aβ generation† Lujia Zhou Department for Developmental and Molecular Genetics, VIB, Leuven, Belgium Center Human KULeuven, Search more papers by this author Nathalie Brouwers Neurodegenerative Brain Diseases Group, of Antwerpen, Laboratory Neurogenetics, Institute Born-Bunge, University Antwerp, Iryna Benilova Annelies Vandersteen Switch Laboratory,...

10.1002/emmm.201100138 article EN cc-by EMBO Molecular Medicine 2011-03-10

Scope Investigations into the immunological response of proteins is often masked by lipopolysaccharide (LPS) contamination. We report an optimized Triton X-114 (TX-114) based LPS extraction method for β-lactoglobulin (BLG) and soy protein extract suitable cell-based assays. Methods results Optimization existing TX-114 phase resulted in >99% reduction levels. However, remaining was found to interfere with concentration assays decreased viability THP-1 macrophages HEK-Blue 293 cells. Upon...

10.1371/journal.pone.0173778 article EN cc-by PLoS ONE 2017-03-29

Organ-on-chip devices are intensively studied in academia and industry due to their high potential pharmaceutical biomedical applications. However, most of the existing organ-on-chip models focus on proof concept individual functional units without possibility testing multiple experimental stimuli parallel. Here we developed a polydimethylsiloxane (PDMS) multiplexed chip with eight parallel channels branching from common access port through which all can be addressed simultaneously need for...

10.1039/d0lc00399a article EN cc-by Lab on a Chip 2020-01-01

Abstract In this article we show how various degrees of glycosylation can be used to control the thermal stability proteins. The primary amines β‐lactoglobulin were glycosylated with glucose or fructose within a range non‐denaturing reaction parameters. modified fractions characterized and analyzed for structural hydrophobic exposure. modification procedure gave rise production glycoproteins well‐defined Gaussian distribution, where appeared more reactive than fructose. integrity secondary,...

10.1002/bit.20030 article EN Biotechnology and Bioengineering 2004-02-12

Alpha-synuclein is a small cytosolic protein involved in the pathogenesis of Parkinson's disease and other neurodegenerative disorders. Recent studies suggested lipid-related function for this brain-enriched protein. Since brain carries high level docosahexaenoic acid (DHA) since extent alpha-synuclein gene expression increases response to DHA intake, we have investigated interaction with essential omega-3 fatty acid. We show that allows be present soluble rather than micellar form. Upon...

10.1021/bi061743l article EN Biochemistry 2006-12-01

Protein glycation causes loss-of-function through a process that has been associated with several diabetic-related diseases. Additionally, hypothesized as promoter of protein aggregation, which could explain the observed link between hyperglycaemia and development aggregating Despite its relevance in range diseases, mechanism induces aggregation remains unknown. Here we describe molecular basis how is linked to by applying variety complementary techniques study nonenzymatic hen lysozyme...

10.1021/bm501077j article EN Biomacromolecules 2014-07-24

Apolipoprotein E ( APOE ) genotype determines Alzheimer's disease AD susceptibility, with the ε4 allele being an established risk factor for late‐onset . The ApoE lipidation status has been reported to impact amyloid‐beta (Aβ) peptide metabolism. details of how affects behavior remain be elucidated. In this study, we prepared lipid‐free and lipid‐bound particles, mimicking high‐density lipoprotein particles found in vivo , all three isoforms (ApoE2, ApoE3, ApoE4) biophysically characterized...

10.1002/1873-3468.13428 article EN cc-by FEBS Letters 2019-05-06

The aggregation of the protein α-synuclein (aSyn) into amyloid fibrils in human brain is associated with development several neurodegenerative diseases, including Parkinson's disease. previously observed prion-like spreading aSyn throughout and finding that heterologous cross-seeding occurs vitro for some proteins suggest exposure to amyloids general may pose a risk disease development. To elucidate which fibril characteristics determine if how seeding can occur, we investigated potential...

10.1016/j.jbc.2021.100358 article EN cc-by Journal of Biological Chemistry 2021-01-01

The aim of this work is to evaluate the impact sulfhydryl groups on ovalbumin aggregation and gelation. Ovalbumin was chemically modified add in various degrees. rate not affected by introduction groups, disulfide bond formation preceded physical interactions. Hence, interactions may be driving force for ovalbumin. Investigation aggregates gels electron microscopy rheology suggested that a critical number can introduced beyond which microstructure transforms from fibrillar into amorphous....

10.1021/jf0601923 article EN Journal of Agricultural and Food Chemistry 2006-06-21

The biological function of α-Synuclein has been related to binding lipids and membranes but these interactions can also mediate aggregation, which is associated Parkinson's disease other neuropathologies. In brain tissue constitutively N-acetylated, a modification that plays an important role in its conformational propensity, lipid membrane binding, aggregation propensity. We studied the lipid-mimetic SDS with N-acetylated non-acetylated α-Synuclein, as well their early-onset variants A30P,...

10.1371/journal.pone.0178576 article EN cc-by PLoS ONE 2017-05-31
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