New Hypothesis Insight of Structural Properties on Four Tau Peptide Fragments in Alzheimer's Disease: Origin from the Histidine Behaviors

• Published in: Chemistry : a European journal Vol. 29; no. 37; pp. e202300868 - n/a
• Main Authors: Sun, Yue, Li, Changgui, Wang, Jinping, Shi, Hu
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 03.07.2023
• Subjects: AD pathogenesis; aggregation mechanism; Alzheimer Disease; Alzheimer's disease; Amino acids; Antifungal agents; Bonding strength; Chemistry; deprotonated and protonated states; Folding; Fragments; Histidine; Histidine - chemistry; histidine behaviors; Humans; Hypotheses; Imidazole; Models, Molecular; Neurodegenerative diseases; Peptide Fragments - chemistry; Peptides; Protein folding; protein folding and misfolding; Protein Structure, Tertiary; Proteins; Protonation; Residues; Tau protein; tau Proteins - chemistry; aggregation mechanism; protein folding and misfolding; AD pathogenesis; histidine behaviors; deprotonated and protonated states

During protein folding and misfolding, structural properties and aggregation tendency can be significantly influenced by histidine behaviors (tautomeric behaviors and protonation behaviors). The original reasons were derived from the net charge changes and the various N/N−H orientation on imidazole...