Aminopeptidase in human CSF which degrades delta-sleep inducing peptide (DSIP).
Nyberg. F F; Thörnwall. M M; Hetta. J J
Key Findings
- An aminopeptidase in CSF can degrade DSIP, reducing its availability.
- The enzyme has an apparent molecular weight of ~80 kDa and is most active at neutral pH.
- Its activity is inhibited by amastatin, bestatin, and EDTA, and it also breaks down enkephalins.
Practical Outcomes
- Because DSIP is rapidly broken down by this enzyme, its effects may be short‑lived when administered intrathecally or systemically. Biohackers might need to use higher or more frequent dosing, or explore formulations that protect DSIP from enzymatic degradation. However, the known inhibitors are not safe for routine use, so direct inhibition isn’t a practical strategy yet.
Summary
Researchers isolated an enzyme in human cerebrospinal fluid that breaks down the sleep‑inducing peptide DSIP. The enzyme is about 80 kDa, works best at neutral pH, and is blocked by compounds like amastatin, bestatin, and EDTA. It also degrades other brain peptides such as enkephalins.
Abstract
This study describes the purification and characterization of an aminopeptidase from human cerebrospinal fluid capable of degrading delta-sleep-inducing-peptide (DSIP). The enzyme has an apparent molecular weight of approximately 80,000 dalton. It is sensitive towards amastatin, bestatin and EDTA and is optimally active at neutral pH. The recovered enzyme was also found to degrade other neuropeptides, e.g., the enkephalins.
Study Information
pubmed
1990
1990-03-30T00:00:00.000Z
10.1016/0006-291x(90)90659-b