Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6

In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* (275)VQIINK(280) and PHF (306)VQIVYK(311) as β-sheets. To understand the role of the constituent amino acids of PHF and...

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Autores principales: Dangi, Abha, Balmik, Abhishek Ankur, Ghorpade, Archana Kisan, Gorantla, Nalini Vijay, Sonawane, Shweta Kishor, Chinnathambi, Subashchandrabose, Marelli, Udaya Kiran
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9055513/
https://www.ncbi.nlm.nih.gov/pubmed/35516938
http://dx.doi.org/10.1039/d0ra03809a
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author Dangi, Abha
Balmik, Abhishek Ankur
Ghorpade, Archana Kisan
Gorantla, Nalini Vijay
Sonawane, Shweta Kishor
Chinnathambi, Subashchandrabose
Marelli, Udaya Kiran
author_facet Dangi, Abha
Balmik, Abhishek Ankur
Ghorpade, Archana Kisan
Gorantla, Nalini Vijay
Sonawane, Shweta Kishor
Chinnathambi, Subashchandrabose
Marelli, Udaya Kiran
author_sort Dangi, Abha
collection PubMed
description In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* (275)VQIINK(280) and PHF (306)VQIVYK(311) as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization.
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spelling pubmed-90555132022-05-04 Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6 Dangi, Abha Balmik, Abhishek Ankur Ghorpade, Archana Kisan Gorantla, Nalini Vijay Sonawane, Shweta Kishor Chinnathambi, Subashchandrabose Marelli, Udaya Kiran RSC Adv Chemistry In Alzheimer's disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occurs via the interaction of two hexapeptide motifs PHF* (275)VQIINK(280) and PHF (306)VQIVYK(311) as β-sheets. To understand the role of the constituent amino acids of PHF and PHF* in the aggregation, a set of 12 alanine mutant peptides was synthesized by replacing each amino acid in PHF and PHF* with alanine and they were characterized by nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), transmission electron microscopy (TEM) and ThS/ANS fluorescence assay. Our studies show that while the aggregation was suppressed in most of the alanine mutant peptides, replacement of glutamine by alanine in both PHF and PHF* enhanced the fibrillization. The Royal Society of Chemistry 2020-07-21 /pmc/articles/PMC9055513/ /pubmed/35516938 http://dx.doi.org/10.1039/d0ra03809a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Dangi, Abha
Balmik, Abhishek Ankur
Ghorpade, Archana Kisan
Gorantla, Nalini Vijay
Sonawane, Shweta Kishor
Chinnathambi, Subashchandrabose
Marelli, Udaya Kiran
Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title_full Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title_fullStr Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title_full_unstemmed Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title_short Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6* and AcPHF6
title_sort residue-based propensity of aggregation in the tau amyloidogenic hexapeptides acphf6* and acphf6
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9055513/
https://www.ncbi.nlm.nih.gov/pubmed/35516938
http://dx.doi.org/10.1039/d0ra03809a
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