@article {46773,
	title = {Residue-based propensity of aggregation in the Tau amyloidogenic hexapeptides AcPHF6*and AcPHF6},
	journal = {RSC Advances},
	volume = {10},
	year = {2020},
	month = {JUL},
	pages = {27331-27335},
	type = {Article},
	abstract = {<p>In Alzheimer{\textquoteright}s disease and related tauopathies, the aggregation of microtubule-associated protein, Tau, into fibrils occursviathe interaction of two hexapeptide motifs PHF*(275)VQIINK(280)and PHF(306)VQIVYK(311)as beta-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.</p>
},
	doi = {10.1039/d0ra03809a},
	author = {Dangi, Abha and Balmik, Abhishek Ankur and Ghorpade, Archana Kisan and Gorantla, Nalini Vijay and Sonawane, Shweta Kishor and Chinnathambi, Subashchandrabose and Marelli, Udaya Kiran}
}
