Premium
Identification and Nanomechanical Characterization of the HIV Tat‐Amyloid β Peptide Multifibrillar Structures
Author(s) -
Feng Qiying,
Hong Yue,
Pradeep Nidamanuri Naga,
Yang Chuanxu,
Li Qiang,
Dong Mingdong
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201905715
Subject(s) - peptide , transactivation , fibril , human immunodeficiency virus (hiv) , amyloid fibril , chemistry , biophysics , amyloid (mycology) , structural protein , atomic force microscopy , microbiology and biotechnology , biology , amyloid β , virology , biochemistry , disease , transcription factor , nanotechnology , materials science , medicine , pathology , gene , inorganic chemistry
HIV transactivator of transcription (Tat) protein could interact with amyloid β (Aβ) peptide which cause the growth of Aβ plaques in the brain and result in Alzheimer's disease in HIV‐infected patients. Herein, we employ high‐resolution atomic force microscopy and quantitative nanomechanical mapping to investigate the effects of Tat protein in Aβ peptide aggregation. Our results demonstrate that the Tat protein could bind to the Aβ fibril surfaces and result in the formation of Tat‐Aβ multifibrillar structures. The resultant Tat‐Aβ multifibrillar aggregates represent an increase in stiffness compared with Aβ fibrils due to the increase in β‐sheet formation. The identification and characterization of the Tat‐Aβ intermediate aggregates is important to understanding the interactions between Tat protein and Aβ peptide, and the development of novel therapeutic strategy for Alzheimer's disease‐like disorder in HIV infected individuals.