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Updated: May 13, 2026
Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Myelin basic protein: structural characterization of spherulites formation and preventive action of trehalose
Cinzia Di Salvo1, Davide Barreca, Giuseppina Laganà
1Dipartimento di Scienze Chimiche, Università di Messina, Viale F. Stagno d'Alcontres 31, 98166 Messina, Italy.
Abstract:
Myelin basic protein (MBP) is one of the main protein components of central nervous system that as shown in our work, under appropriate condition, forms spherulites. The structural and morphological features of these elements and the ability of trehalose to decrease or completely avoid their formation have been clarified with different but complementary techniques. The FTIR spectra provided compelling evidence for the presence of a small amount of elements organized in secondary structures such as helices and sheets. Polarized optical microscope observations show the presence of spherulites with an average size ranged from 41 to 61 μm, characterized by non-birifrangent core. The fluorescence data supply useful informations that are consistent with the presence of a molecular exclusion effect, following interaction of the disaccharide with protein that involves the environment around the single tryptophan residue. Moreover, study of protein conformational states by SDS-PAGE, let us to state that trehalose completely avoid autocatalytic cleavage properties of MBP up to 4 days of incubation at 37 °C and pH 7.4.
Insights
Trehalose prevents the formation of myelin basic protein (MBP) spherulites and preserves protein structure. This finding is crucial for understanding and stabilizing central nervous system proteins.
Area of Science:
- Biochemistry
- Neuroscience
- Materials Science
Background:
- Myelin basic protein (MBP) is a key component of the central nervous system's myelin sheath.
- Under specific conditions, MBP can self-assemble into spherulites, potentially impacting its function.
- Understanding protein aggregation and stabilization is vital for neurological research.
Purpose of the Study:
- To investigate the formation of MBP spherulites.
- To elucidate the structural and morphological characteristics of these spherulites.
- To determine the effect of trehalose on MBP spherulite formation and protein stability.
Main Methods:
- Fourier Transform Infrared (FTIR) spectroscopy to analyze secondary structures.
- Polarized optical microscopy to observe spherulite morphology and size.
- Fluorescence spectroscopy to study protein-disaccharide interactions.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to assess protein conformational changes.
Main Results:
- FTIR confirmed the presence of helical and sheet structures in MBP.
- Polarized optical microscopy revealed non-birefringent core spherulites ranging from 41 to 61 μm.
- Fluorescence data indicated a molecular exclusion effect upon trehalose interaction with MBP.
- SDS-PAGE demonstrated that trehalose completely inhibited MBP autocatalytic cleavage for up to 4 days.
Conclusions:
- Trehalose effectively prevents the formation of myelin basic protein spherulites.
- Trehalose stabilizes MBP, preserving its structure and preventing degradation.
- These findings offer insights into stabilizing CNS proteins and preventing aggregation-related pathologies.
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