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2 results on '"modified Aβ peptide fragments"'

1. Aluminium Binding to Modified Amyloid-β Peptides: Implications for Alzheimer’s Disease

Author

Monica Jureschi, Cosmin Stefan Mocanu, and Gabi Drochioiu

Subjects
Models, Molecular, Circular dichroism, Protein Conformation, Proton Magnetic Resonance Spectroscopy, Pharmaceutical Science, Peptide, Microscopy, Atomic Force, 01 natural sciences, amyloid-β peptides, Analytical Chemistry, Serine, chemistry.chemical_compound, Drug Discovery, Spectroscopy, Fourier Transform Infrared, Peptide synthesis, aluminium ions, mass spectrometry, Alanine, chemistry.chemical_classification, 0303 health sciences, atomic force microscopy, Circular Dichroism, Hydrogen-Ion Concentration, circular dichroism spectroscopy, Chemistry (miscellaneous), Molecular Medicine, Alzheimer’s disease, Protein Binding, Stereochemistry, Article, lcsh:QD241-441, 03 medical and health sciences, Ion binding, lcsh:Organic chemistry, Alzheimer Disease, Amino Acid Sequence, Physical and Theoretical Chemistry, Histidine, 030304 developmental biology, Ions, Amyloid beta-Peptides, 010405 organic chemistry, Organic Chemistry, metal binding, modified Aβ peptide fragments, 0104 chemical sciences, FT-IR, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Glycine, Aluminum
Abstract

Aluminium (Al) is clearly neurotoxic and considerable evidence exists that Al may play a role in the aetiology or pathogenesis of Alzheimer&rsquo, s disease (AD). Nevertheless, the link between AD pathology and Al is still open to debate. Therefore, we investigated here the interaction of aluminium ions with two A&beta, peptide fragments and their analogues. First, we synthesised by the Fmoc/tBu solid-phase peptide synthesis (SPPS) strategy using an automated peptide synthesiser two new peptides starting from the A&beta, (1&ndash, 16) native peptide fragment. For this purpose, the three histidine residues (H6, H13, and H14) of the A&beta, 16) peptide were replaced by three alanine and three serine residues to form the modified peptides A&beta, 16)A36,13,14 and A&beta, 16)S36,13,14 (primary structures: H-1DAEFRADSGYEVAAQK16-NH2 and H-1DAEFRSDSGYEVSSQK16-NH2). In addition, the A&beta, (9&ndash, 16) peptide fragment (H-9GYEVHHQK16-NH2) and its glycine analogues, namely A&beta, 16)G110, (H-9GGEVHHQK16-NH2), A&beta, 16)G213,14 (H-9GYEVGGQK16-NH2), and A&beta, 16)G310,13,14 (H-9GGEVGGQK16-NH2), were manually synthesised in order to study Al binding to more specific amino acid residues. Both the peptides and the corresponding complexes with aluminium were comparatively investigated by mass spectrometry (MS), circular dichroism spectroscopy (CD), atomic force microscopy (AFM), scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FT-IR). Al&ndash, peptide molecular ions and Al-fragment ions were unambiguously identified in the MS and MS/MS spectra. AFM images showed dramatic changes in the film morphology of peptides upon Al binding. Our findings from the investigation of N-terminal 1-16 and even 9-16 normal and modified sequences of A&beta, peptides suggest that they have the capability to be involved in aluminium ion binding associated with AD.

Published
2020
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2. Aluminium Binding to Modified Amyloid-β Peptides: Implications for Alzheimer's Disease.

Author

Mocanu, Cosmin Stefan, Jureschi, Monica, Drochioiu, Gabi, D'Andrea, Luca D., and Rosa, Lucia De

Subjects
*ALZHEIMER'S disease, *GLYCINE, *PEPTIDES, *FOURIER transform infrared spectroscopy, *AMYLOID beta-protein, *ALUMINUM, *ATOMIC force microscopy
Abstract

Aluminium (Al) is clearly neurotoxic and considerable evidence exists that Al may play a role in the aetiology or pathogenesis of Alzheimer's disease (AD). Nevertheless, the link between AD pathology and Al is still open to debate. Therefore, we investigated here the interaction of aluminium ions with two Aβ peptide fragments and their analogues. First, we synthesised by the Fmoc/tBu solid-phase peptide synthesis (SPPS) strategy using an automated peptide synthesiser two new peptides starting from the Aβ(1–16) native peptide fragment. For this purpose, the three histidine residues (H6, H13, and H14) of the Aβ(1–16) peptide were replaced by three alanine and three serine residues to form the modified peptides Aβ(1–16)A36,13,14 and Aβ(1–16)S36,13,14 (primary structures: H-1DAEFRADSGYEVAAQK16-NH2 and H-1DAEFRSDSGYEVSSQK16-NH2). In addition, the Aβ(9–16) peptide fragment (H-9GYEVHHQK16-NH2) and its glycine analogues, namely Aβ(9–16)G110, (H-9GGEVHHQK16-NH2), Aβ(9–16)G213,14 (H-9GYEVGGQK16-NH2), and Aβ(9–16)G310,13,14 (H-9GGEVGGQK16-NH2), were manually synthesised in order to study Al binding to more specific amino acid residues. Both the peptides and the corresponding complexes with aluminium were comparatively investigated by mass spectrometry (MS), circular dichroism spectroscopy (CD), atomic force microscopy (AFM), scanning electron microscopy (SEM), and Fourier transform infrared spectroscopy (FT-IR). Al–peptide molecular ions and Al-fragment ions were unambiguously identified in the MS and MS/MS spectra. AFM images showed dramatic changes in the film morphology of peptides upon Al binding. Our findings from the investigation of N-terminal 1-16 and even 9-16 normal and modified sequences of Aβ peptides suggest that they have the capability to be involved in aluminium ion binding associated with AD. [ABSTRACT FROM AUTHOR]

Published
2020
Full Text
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