β-Endorphin: Formation of α-helix in lipid solutions

C. S.C. Wu, N. M. Lee, H. H. Loh, J. T. Yang, C. H. Li

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

Human β-endorphin adopts a partial helical conformation in aqueous solutions of cerebroside sulfate, ganglioside GM1, phosphatidylserine, and phosphatidic acid, but not of cerebroside and phosphatidylcholine, as evidenced by circular dichroic spectra. Addition of Ca2+ to the peptide in cerebroside sulfate solution can break up the helix; at 10 mM Ca2+ the peptide (12 μM) essentially exists in an unordered form. For comparison, sheep β-lipotropin in acidic cerebroside sulfate solution (pH < 4) also has a partial helical conformation, whereas human adrenocorticotropin does not. The conformation of the complex between human β-endorphin and lipids may be related to the opiatelike function of this peptide hormone.

Original languageEnglish (US)
Pages (from-to)3656-3659
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number8
DOIs
StatePublished - 1979

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