Soricidin
Soricidin is a peptide that was originally derived from the saliva of the Northern Short-tailed Shrew (Blarina brevicauda). It is known for its potential in the treatment of various types of cancer, particularly ovarian cancer and pancreatic cancer.
Origin[edit | edit source]
Soricidin was first identified in the saliva of the Northern Short-tailed Shrew, a small mammal native to North America. The shrew uses this peptide as a paralytic agent to immobilize its prey. The peptide was isolated and its structure was determined by researchers studying the shrew's unique hunting methods.
Structure and Function[edit | edit source]
Soricidin is a 54-amino acid peptide. It functions by binding to and inhibiting the activity of TRPV6 calcium channels, which are overexpressed in many types of cancer cells. By inhibiting these channels, soricidin can induce apoptosis, or programmed cell death, in the cancer cells.
Medical Applications[edit | edit source]
Soricidin has shown promise in preclinical studies for the treatment of various types of cancer. It has been found to be particularly effective against ovarian and pancreatic cancers, which are known to overexpress TRPV6 channels.
In addition to its potential as a standalone treatment, soricidin may also be used in combination with other cancer therapies. For example, it may enhance the effectiveness of chemotherapy by increasing the sensitivity of cancer cells to the drugs used in this treatment.
Research and Development[edit | edit source]
Research into the potential medical applications of soricidin is ongoing. Several pharmaceutical companies and research institutions are currently conducting preclinical and clinical trials to further investigate the peptide's effectiveness and safety profile.
See Also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD