NDLI: Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

Content Provider	Springer Nature Link
Author	Arasteh, Amir Habibi Rezaei, Mehran Ebrahim Habibi, Azadeh Moosavi Movahedi, Ali Akbar
Copyright Year	2012
Abstract	Amyloid fibrils are considered as nanostructures that could be formed by ordered self-assembly of the partially-folded states of many different peptides or proteins. In this study, bovine serum albumin was used as a model protein whose ordered aggregation (fibrillation) was optimized. Response surface methodology (RSM) was used in a design that contained a total of 30 experimental trials. The first 24 were organized in a factorial design and from 25 to 30 involved the replications of the central points. Data obtained from RSM were subjected to the analysis of variance (ANOVA) and analyzed using a second order polynomial equation. Subsequent testing of the suggested experimental parameters was done in vitro with Congo red spectrophotometric assay. Protein concentration, pH, temperature and time of incubation were the variables used in this study. Responses were assessed by measuring absorbance in 540 nm (characteristic of amyloid formation) and maximal wavelength. Concomitant effects of variables were assessed in surface plots that each considered two of the variables. Interestingly, the pattern obtained by monitoring absorbance at 540 nm and absorbance in maximal wavelength were identical in most cases. We are reporting the optimum concentration of protein, pH, temperature and time at 5 mg ml$^{−1}$, 3.02 and 72 °C and 48 h, respectively. Our findings suggest that use of Congo red spectrophotometric test, as a simple and affordable assay could be suggested as a first test for assessing fibril formation of proteins. Absorbance in maximal wavelength is recommended as a significant indication of fibril formation.
Starting Page	457
Ending Page	465
Page Count	9
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	31
Issue Number	6
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2012-05-31
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Bovine serum albumin (BSA) Protein aggregation Amyloid Response surface methodology (RSM) Fibrillation Organic Chemistry Animal Anatomy / Morphology / Histology Biochemistry Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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