The thermal and storage stability of bovine haemoglobin by ultra violet–visible and circular dichroism spectroscopies
Bhomia, Ruchir, Trivedi, Vivek ORCID: 0000-0001-9304-9214, Coleman, Nichola J. and Mitchell, John C. ORCID: 0000-0003-2945-3292 (2016) The thermal and storage stability of bovine haemoglobin by ultra violet–visible and circular dichroism spectroscopies. Journal of Pharmaceutical Analysis, 6 (4). pp. 242-248. ISSN 2095-1779 (Print), 2214-0883 (Online) (doi:https://doi.org/10.1016/j.jpha.2016.02.004)
|
PDF (Publisher's PDF - Open Access)
15256_Trivedi_The thermal and storage stability (pub PDF OA) 2016.pdf - Published Version Available under License Creative Commons Attribution Non-commercial No Derivatives. Download (2MB) | Preview |
|
|
PDF (Author's Accepted Manuscript)
15256_TRIVEDI_Investigation of the thermal (AAM) 2016.pdf - Accepted Version Available under License Creative Commons Attribution Non-commercial No Derivatives. Download (497kB) | Preview |
Abstract
The effects of temperature, pH and long-term storage on the secondary structure and conformation changes of bovine haemoglobin (bHb) were studied using circular dichroism (CD) and ultraviolet-visible (UV-vis) spectroscopies. Neural network software was used to deconvolute the CD data to obtain the fractional content of the five secondary structures. The storage stability of bHb solutions in pH 6, 7 and 8 buffers was significantly higher at 4 °C in comparison to 23 °C for the first 3 days. A complete denaturation of bHb was observed after 40 days irrespective of storage temperature or pH. The bHb solutions were also exposed to heating and cooling cycles between 25 and 65 °C and structural changes were followed by UV-vis and CD spectroscopies. These experiments demonstrated that α-helix content of bHb decreases steadily with increasing temperature above 35 °C at all pH values. The loss in α-helicity and gain in random coil conformations was pH-dependent and greatest under alkaline conditions. Furthermore, there was minimal recovery of the secondary structure content upon cooling to 25 °C. The use of bHb as a model drug is very common and this study illustrates the significance of storage and processing conditions on its stability.
Item Type: | Article |
---|---|
Additional Information: | © 2016 Xi'an Jiaotong University. Production and hosting by Elsevier B.V. This is an open access article under the CCBY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
Uncontrolled Keywords: | Bovine haemoglobin, Circular dichroism, Thermal stability, Storage stability |
Faculty / School / Research Centre / Research Group: | Faculty of Engineering & Science Faculty of Education, Health & Human Sciences > School of Human Sciences (HUM) |
Last Modified: | 09 Oct 2021 04:45 |
URI: | http://gala.gre.ac.uk/id/eprint/15256 |
Actions (login required)
View Item |
Downloads
Downloads per month over past year