دورية أكاديمية
أعرض في EDS

Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.

التفاصيل البيبلوغرافية
العنوان: Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.
المؤلفون: Braun GA; Biochemistry and Structural Biology, Lund University Lund Sweden sara.linse@biochemistry.lu.se., Dear AJ; Biochemistry and Structural Biology, Lund University Lund Sweden sara.linse@biochemistry.lu.se.; Department of Cell Biology, Harvard Medical School Boston MA USA.; Paulson School of Engineering and Applied Science, Harvard University Cambridge MA USA.; Department of Chemistry, University of Cambridge Cambridge UK., Sanagavarapu K; Biochemistry and Structural Biology, Lund University Lund Sweden sara.linse@biochemistry.lu.se., Zetterberg H; Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at the University of Gothenburg Mölndal Sweden.; Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital Mölndal Sweden.; Department of Neurodegenerative Disease, UCL Institute of Neurology Queen Square London UK.; UK Dementia Research Institute at UCL London UK., Linse S; Biochemistry and Structural Biology, Lund University Lund Sweden sara.linse@biochemistry.lu.se.
المصدر: Chemical science [Chem Sci] 2022 Feb 07; Vol. 13 (8), pp. 2423-2439. Date of Electronic Publication: 2022 Feb 07 (Print Publication: 2022).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101545951 Publication Model: eCollection Cited Medium: Print ISSN: 2041-6520 (Print) Linking ISSN: 20416520 NLM ISO Abbreviation: Chem Sci Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : Royal Society of Chemistry, [2010]-
مستخلص: The pathology of Alzheimer's disease is connected to the aggregation of β-amyloid (Aβ) peptide, which in vivo exists as a number of length-variants. Truncations and extensions are found at both the N- and C-termini, relative to the most commonly studied 40- and 42-residue alloforms. Here, we investigate the aggregation of two physiologically abundant alloforms, Aβ 37 and Aβ 38 , as pure peptides and in mixtures with Aβ 40 and Aβ 42 . A variety of molar ratios were applied in quaternary mixtures to investigate whether a certain ratio is maximally inhibiting of the more toxic alloform Aβ 42 . Through kinetic analysis, we show that both Aβ 37 and Aβ 38 self-assemble through an autocatalytic secondary nucleation reaction to form fibrillar β-sheet-rich aggregates, albeit on a longer timescale than Aβ 40 or Aβ 42 . Additionally, we show that the shorter alloforms co-aggregate with Aβ 40 , affecting both the kinetics of aggregation and the resulting fibrillar ultrastructure. In contrast, neither Aβ 37 nor Aβ 38 forms co-aggregates with Aβ 42 ; however, both short alloforms reduce the rate of Aβ 42 aggregation in a concentration-dependent manner. Finally, we show that the aggregation of Aβ 42 is more significantly impeded by a combination of Aβ 37 , Aβ 38 , and Aβ 40 than by any of these alloforms independently. These results demonstrate that the aggregation of any given Aβ alloform is significantly perturbed by the presence of other alloforms, particularly in heterogeneous mixtures, such as is found in the extracellular fluid of the brain.
Competing Interests: H. Z. has served at scientific advisory boards for Eisai, Denali, Roche Diagnostics, Wave, Samumed, Siemens Healthineers, Pinteon Therapeutics, Nervgen, AZTherapies and CogRx, has given lectures in symposia sponsored by Cellectricon, Fujirebio, Alzecure and Biogen, and is a co-founder of Brain Biomarker Solutions in Gothenburg AB (BBS), which is a part of the GU Ventures Incubator Program (outside submitted work).
(This journal is © The Royal Society of Chemistry.)
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تواريخ الأحداث: Date Created: 20220321 Latest Revision: 20220322
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8864715
DOI: 10.1039/d1sc02990h
PMID: 35310497
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-6520
DOI:10.1039/d1sc02990h