Degradation and aggregation of delta sleep-inducing peptide (DSIP) and two analogs in plasma and serum
The biostability of DSIP (delta sleep-inducing peptide) and two analogs in blood was investigated in order to determine if rates of inactivation contribute to variable effects in vivo. Incubation of DSIP in human or rat blood led to release of products having retention times on a gel filtration column equivalent to Trp. Formation of products was dependent on temperature, time, and species. Incubation of /sup 125/I-N-Tyr-DSIP and /sup 125/I-N-Tyr-P-DSIP, a phosphorylated analog, revealed slower degradation and, in contrast to DSIP, produced complex formation. An excess of unlabeled material did not displace the radioactivity supporting the assumption of non-specific binding/aggregation. It was concluded that the rapid disappearance of injected DSIP in blood was due to degradation, whereas complex formation together with slower degradation resulted in longer persistence of apparently intact analogs. Whether this could explain the sometimes stronger and more consistent effects of DSIP-analogs remains to be examined.
- Research Organization:
- University Hospital, Basel, Switzerland
- OSTI ID:
- 5977602
- Journal Information:
- Peptides (Fayetteville, N.Y.); (United States), Vol. 8:4
- Country of Publication:
- United States
- Language:
- English
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550501* - Metabolism- Tracer Techniques