Issue 44, 2016

Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

Abstract

Amyloid fibril formation has been seen as the underlying reason for various pathological disorders studied in humans. Understanding the mechanism of amyloid fibril formation is important to prevent the onset or to develop a possible cure. In this study, we have experienced to understand the role of positively charged head and hydrophobic tail of cationic surfactant and its propensity to stimulate amyloid fibril formation in concanavalin A. Several spectroscopic techniques (far-UV CD, FTIR, Rayleigh scattering, turbidity, intrinsic fluorescence, and dye binding assays) in addition to transmission electron microscopy were employed to analyze the mode of interaction between ConA and cetyltrimethylammonium bromide (CTAB) during amyloid fibril formation. We have found that negatively charged ConA at pH 7.4, transforms into amyloid fibril in response to significantly low concentrations of CTAB while higher concentrations abolishes the amyloid fibril formation. Interestingly, ConA at pH 3.5 did not form amyloid fibril at varying concentrations of CTAB. A characteristically unique type of secondary structural transition was seen under the varying concentrations of CTAB. At low CTAB concentrations far-UV CD spectrum minimum shifts towards higher wavelength (222–225 nm) whereas at higher concentrations the β-sheet transformed into α-helical structures which is also evident from FTIR measurements. These results suggest that electrostatics as well as hydrophobic interaction are involved in the CTAB induced amyloid fibril formation. This study opens up the possibilities to understand the molecular mechanism of the interaction between CTAB and ConA and also helps to make a molecule which can inhibit or suppress the amyloid fibrillogenesis.

Graphical abstract: Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

Article information

Article type
Paper
Submitted
09 feb. 2016
Accepted
05 apr. 2016
First published
07 apr. 2016

RSC Adv., 2016,6, 38100-38111

Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

J. M. Khan, M. S. Khan, M. S. Ali, N. A. Al-Shabib and R. H. Khan, RSC Adv., 2016, 6, 38100 DOI: 10.1039/C6RA03707K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements