MAUROCALCIN

Product Name: MAUROCALCIN

Purity: 95%

Molar Mass: 3859.0

Chemical Formula: C156H260N56O46S6

Synonyms: MCa, Maurocalcin

Storage: Store at -20 degrees Celsius

Sequence: GDCLPHLKLCKENKDCCSKKCKRRGTNIEKRCR

Application:

Maurocalcin is a peptide toxin derived from the venom of the scorpion Scorpio maurus palmatus. It specifically targets and modulates ryanodine receptors (RyR), which are critical for calcium ion release in muscle cells. By binding to these receptors, Maurocalcin enhances calcium ion influx, leading to potent activation of intracellular calcium signaling pathways. This unique mechanism positions Maurocalcin as a valuable tool in studying calcium dynamics and muscle physiology. Additionally, its potential therapeutic applications include the treatment of conditions involving dysfunctional calcium homeostasis, such as certain muscle disorders and cardiac arrhythmias.

Current Research:

Maurocalcine, a 33-amino-acid peptide derived from the venom of Scorpio maurus palmatus, has gained prominence in drug discovery due to its high affinity for ryanodine receptors (RyRs). As a potent modulator of calcium channels, maurocalcine interacts specifically with RyR1, the skeletal muscle isoform, inducing channel activation and prolonged open states. This unique functionality makes it a valuable tool for exploring calcium signaling pathways and developing therapeutic interventions for calcium-related disorders.

The peptide’s structural and functional properties are of significant academic interest. Maurocalcine adopts a compact, disulfide-rich structure stabilized by three disulfide bridges, contributing to its exceptional stability and specificity. Its ability to mimic the cytoplasmic domain of the ryanodine receptor facilitates detailed studies of RyR conformational dynamics, providing insights into calcium release mechanisms crucial for muscle contraction, cardiac function, and neuronal signaling.

In biomedical research, maurocalcine is being explored for its potential in targeting calcium dysregulation, a hallmark of various pathological conditions. Studies suggest its role in uncovering therapeutic targets for muscle disorders, including malignant hyperthermia and certain myopathies associated with RyR mutations. Its impact on intracellular calcium homeostasis also positions maurocalcine as a candidate for studying neurodegenerative diseases, where calcium signaling is often disrupted.

Synthetic analogs of maurocalcine are being developed to improve pharmacological properties and reduce venom-derived toxicity. These modifications aim to enhance receptor specificity and therapeutic viability, broadening the peptide's application in drug development.

For researchers, maurocalcine serves as a critical probe for dissecting RyR function and calcium-mediated signaling pathways. Its potential as both a research tool and a therapeutic lead underscores its importance in advancing our understanding of calcium regulation and its implications for treating diverse diseases.

Reference:

Ronjat, M., Feng, W., Dardevet, L., Dong, Y., Al Khoury, S., Chatelain, F. C., … & De Waard, M. (2016). In cellulo phosphorylation induces pharmacological reprogramming of maurocalcin, a cell-penetrating venom peptide. Proceedings of the National Academy of Sciences, 113(17), E2460-E2468.