MBP

MBP Full Name

myelin basic protein

MBP Introduction

Myelin basic protein (MBP) is one of the most abundant structural proteins in the myelin sheath of the central nervous system and plays a fundamental role in maintaining the compact architecture of myelin that surrounds neuronal axons. Myelin acts as an electrical insulator, enabling rapid saltatory conduction of nerve impulses along axons, and disruptions to this structure are closely associated with neurological dysfunction. MBP is encoded by the MBP gene and is primarily expressed by oligodendrocytes in the central nervous system. Unlike many structured proteins, MBP belongs to the class of intrinsically disordered proteins (IDPs), meaning it lacks a fixed three-dimensional conformation under physiological conditions. This structural flexibility allows MBP to interact dynamically with a variety of molecular partners, including negatively charged lipids and other myelin-associated proteins, making it a critical component for forming the "major dense line" that stabilizes tightly packed myelin layers.

Figure 1. Loss of Myelin Basic Protein Function Triggers Myelin Breakdown in Models of Demyelinating Diseases.(Sources: Weil MT, et al.; 2016)

Functionally, MBP acts as a molecular "adhesive" that promotes the compaction and stability of the myelin membrane. Its positively charged domains bind strongly to negatively charged phospholipids in the myelin bilayer, drawing adjacent membrane surfaces together and maintaining the multilamellar structure required for efficient nerve conduction. Recent experimental and computational studies have further clarified how MBP achieves this function. Although intrinsically disordered in solution, MBP can adopt transient, more ordered conformations upon interacting with lipid membranes, enabling membrane adhesion and structural organization. Research using biomimetic myelin membrane systems has demonstrated that MBP can actively trigger adhesion between lipid bilayers, effectively recreating key aspects of myelin formation In Vitro. In addition, post-translational modifications of MBP—such as phosphorylation, methylation, and deimination—are known to regulate its interaction with lipids and proteins, influencing myelin stability and remodeling during development or repair processes.

From a disease perspective, MBP has long been recognized as a central molecule in demyelinating and neuroinflammatory disorders. Alterations in MBP expression, structure, or post-translational modification are strongly linked to diseases such as multiple sclerosis (MS), experimental autoimmune encephalomyelitis (EAE), and other forms of central nervous system demyelination. In autoimmune conditions, MBP can act as an antigen that triggers immune responses against myelin, leading to progressive myelin damage and neurological impairment. Because of this, MBP is widely used as a biomarker and experimental target in studies investigating myelin degeneration, immune-mediated neuroinflammation, and strategies for remyelination therapy. Increasingly, advances in biomimetic membrane systems, structural prediction tools, and neurobiological research are providing deeper insight into how MBP regulates myelin assembly and repair, offering potential avenues for developing therapies aimed at restoring myelin integrity in neurological diseases.

Alternate Names for MBP

MBP; myelin basic protein; myelin A1 protein; microtubule-stabilizing protein; 20 kDa microtubule-stabilizing protein;

• Neurologic Diseases Catalogue

• 1.Kister A, Kister I. Overview of myelin, major myelin lipids, and myelin-associated proteins. Front Chem. 2023, 10:1041961.
  2.Krugmann B, et al.; Adhesion Process of Biomimetic Myelin Membranes Triggered by Myelin Basic Protein. Front Chem. 2021, 9:631277.
  3.Weil MT, et al.; Loss of Myelin Basic Protein Function Triggers Myelin Breakdown in Models of Demyelinating Diseases. Cell Rep. 2016, 16(2):314-322.