Cationic gemini surfactant stimulates amyloid fibril formation in bovine liver catalase at physiological pH. A biophysical study
نویسندگان
چکیده
منابع مشابه
Biophysical Studies on the Interaction of Insulin with a Cationic Gemini Surfactant
A novel quaternary ammonium-based cationic gemini surfactant (S6) having 1,6 di-bromo hexane as a spacer, have been used and its interaction with insulin in aqueous solution (pH, 7.40) was investigated by several methods including fluorescence spectroscopy, UV-Vis spectroscopy, circular dichroism, dynamic light scattering, ζ-potential measurements, conductivity and transmission electron microsc...
متن کاملbiophysical studies on the interaction of insulin with a cationic gemini surfactant
a novel quaternary ammonium-based cationic gemini surfactant (s6) having 1,6 di-bromo hexane as a spacer, have been used and its interaction with insulin in aqueous solution (ph, 7.40) was investigated by several methods including fluorescence spectroscopy, uv-vis spectroscopy, circular dichroism, dynamic light scattering, ζ-potential measurements, conductivity and transmission electron microsc...
متن کاملSpontaneous aggregate transition in mixtures of a cationic gemini surfactant with a double-chain cationic surfactant.
Controllable aggregate transitions were realized by mixing two kinds of cationic surfactants, hexylene-1,6-bis(dodecyldimethylammonium bromide) (C(12)C(6)C(12)Br(2)) and didodecyldimethylammonium bromide (DDAB). It was found that two parameters are the main factors determining the aggregation behavior of the mixed system, the total concentration of DDAB and C(12)C(6)C(12)Br(2) (C(T)), and the m...
متن کاملInsights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence
Human insulin is a widely used model protein for the study of amyloid formation as both associated to insulin injection amyloidosis in type II diabetes and highly prone to form amyloid fibrils in vitro. In this study, we aim to gain new structural insights into insulin fibril formation under two different aggregating conditions at neutral and acidic pH, using a combination of fluorescence, circ...
متن کاملThe role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH
RATIONALE Amyloid formation is implicated in a number of human diseases. β(2)-Microglobulin (β(2)m) is the precursor protein in dialysis-related amyloidosis and it has been shown that partial, or more complete, unfolding is key to amyloid fibril formation in this pathology. Here the relationship between conformational flexibility and β(2)m amyloid formation at physiological pH has been investig...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: RSC Advances
سال: 2020
ISSN: 2046-2069
DOI: 10.1039/d0ra07560d