Next Article in Journal
BAMBI Promotes C2C12 Myogenic Differentiation by Enhancing Wnt/β-Catenin Signaling
Next Article in Special Issue
Monitoring of Intracellular Tau Aggregation Regulated by OGA/OGT Inhibitors
Previous Article in Journal
Evaluation of Antioxidant, Antidiabetic and Anticholinesterase Activities of Smallanthus sonchifolius Landraces and Correlation with Their Phytochemical Profiles
Previous Article in Special Issue
Protein Folding and Mechanisms of Proteostasis
Open AccessArticle

Colloidal Stability & Conformational Changes in β-Lactoglobulin: Unfolding to Self-Assembly

Malvern Instruments, 7221 Lee Deforest Drive, Suite 300, Columbia, MD 21046, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Salvador Ventura
Int. J. Mol. Sci. 2015, 16(8), 17719-17733; https://doi.org/10.3390/ijms160817719
Received: 2 July 2015 / Revised: 23 July 2015 / Accepted: 27 July 2015 / Published: 3 August 2015
(This article belongs to the Collection Protein Folding)
A detailed understanding of the mechanism of unfolding, aggregation, and associated rheological changes is developed in this study for β-Lactoglobulin at different pH values through concomitant measurements utilizing dynamic light scattering (DLS), optical microrheology, Raman spectroscopy, and differential scanning calorimetry (DSC). The diffusion interaction parameter kD emerges as an accurate predictor of colloidal stability for this protein consistent with observed aggregation trends and rheology. Drastic aggregation and gelation were observed at pH 5.5. Under this condition, the protein’s secondary and tertiary structures changed simultaneously. At higher pH (7.0 and 8.5), oligomerizaton with no gel formation occurred. For these solutions, tertiary structure and secondary structure transitions were sequential. The low frequency Raman data, which is a good indicator of hydrogen bonding and structuring in water, has been shown to exhibit a strong correlation with the rheological evolution with temperature. This study has, for the first time, demonstrated that this low frequency Raman data, in conjunction with the DSC endotherm, can be been utilized to deconvolve protein unfolding and aggregation/gelation. These findings can have important implications for the development of protein-based biotherapeutics, where the formulation viscosity, aggregation, and stability strongly affects efficacy or in foods where protein structuring is critical for functional and sensory performance. View Full-Text
Keywords: dynamic light scattering; differential scanning calorimetry; Raman spectroscopy; self-assembly; protein aggregation; protein unfolding; microrheology dynamic light scattering; differential scanning calorimetry; Raman spectroscopy; self-assembly; protein aggregation; protein unfolding; microrheology
Show Figures

Graphical abstract

MDPI and ACS Style

Blake, S.; Amin, S.; Qi, W.; Majumdar, M.; Lewis, E.N. Colloidal Stability & Conformational Changes in β-Lactoglobulin: Unfolding to Self-Assembly. Int. J. Mol. Sci. 2015, 16, 17719-17733.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Search more from Scilit
 
Search
Back to TopTop