Covalent defects restrict supramolecular self-assembly of homopolypeptides: case study of β2-fibrils of poly-L-glutamic acid

• Published in: PloS one Vol. 9; no. 8; p. e105660
• Main Authors: Fulara, Aleksandra, Hernik, Agnieszka, Nieznańska, Hanna, Dzwolak, Wojciech
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 21.08.2014; Public Library of Science (PLoS)
• Subjects: Acids; Aggregates; Amyloid; Amyloid - chemistry; Bifurcations; Biology and Life Sciences; Biomaterials; Biomedical materials; Carbodiimide; Case reports; Case studies; Chains; Chemical bonds; Chemistry; Conformation; Correlation analysis; Covalence; Defects; Electron microscopy; Electrostatic properties; Electrostatics; Engineering and Technology; Fibrillogenesis; Fourier transforms; Glutamic acid; Hydrogen; Hydrogen bonding; Hydrogen bonds; Hydrogen ion concentration; Infrared absorption; Infrared spectroscopy; Lactic Acid - chemistry; Microscopy; Physical Sciences; Polyglutamic Acid - chemistry; Polyglycolic Acid - chemistry; Polylactide-co-glycolide; Polylysine; Polypeptides; Proteins; Red shift; Research and Analysis Methods; Self assembly; Studies; Poland

Poly-L-glutamic acid (PLGA) often serves as a model in studies on amyloid fibrils and conformational transitions in proteins, and as a precursor for synthetic biomaterials. Aggregation of PLGA chains and formation of amyloid-like fibrils was shown to continue on higher levels of superstructural self...