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Degradation and aggregation of delta sleep-inducing peptide (DSIP) and two analogs in plasma and serum

Study · human · Peptides · 1987 · DOI 10.1016/0196-9781(87)90031-3 · PMID 3628078

Plain-language summary

Paraphrased from the published abstract below — not a verdict on whether anything works.

In this study using human and rat blood, researchers investigated the biostability of DSIP (delta sleep-inducing peptide) and two analogs. Incubating DSIP in blood produced degradation products with retention times on a gel filtration column matching Trp, with formation depending on temperature, time, and species. Incubating 125I-N-Tyr-DSIP and the phosphorylated analog 125I-N-Tyr-P-DSIP showed slower degradation and, unlike DSIP, produced complex formation; excess unlabeled material did not displace the radioactivity, consistent with non-specific binding/aggregation. The authors conclude the rapid disappearance of injected DSIP in blood was due to degradation, while complex formation together with slower degradation resulted in longer persistence of the analogs, and note this might help explain differences in the reported strength and consistency of DSIP-analog effects.

Abstract

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 125I-N-Tyr-DSIP and 125I-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.

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