Neuropeptides interact with glycolipid receptors A surface plasmon resonance study

Using Surface Plasmon Resonance (SPR) we investigated the interaction of seven neuropeptides with different characteristics and β-amyloid (Aβ42) peptide, with membranes containing gangliosides. A wide range of affinities characterized the bindings (K D = 10 −3– 10 −7 M), following the scheme: for GM...

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Published inPeptides (New York, N.Y. : 1980) Vol. 22; no. 7; pp. 1099 - 1106
Main Authors Valdes-Gonzalez, Tania, Inagawa, Junichi, Ido, Tatsuo
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.07.2001
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Summary:Using Surface Plasmon Resonance (SPR) we investigated the interaction of seven neuropeptides with different characteristics and β-amyloid (Aβ42) peptide, with membranes containing gangliosides. A wide range of affinities characterized the bindings (K D = 10 −3– 10 −7 M), following the scheme: for GM1, Aβ42 > DYN > SP = GAL = SOM = BRD > OXY = ENK; for GD1a, Aβ42 = DYN = GAL > SP = SOM = BRD = OXY > ENK and for GT1b, Aβ42 > DYN > SP = GAL > SOM = BRD = OXY > ENK. The ganglioside sugar moiety, specifically the sialic acid, had an important role in the interactions. In general the affinities were higher with polysialo, than with monosialo gangliosides. The sensorgrams describing the interactions of Aβ42 and SP with gangliosides differed from the interactions of the other studied peptides. Ca 2+ promoted changes in peptide-glycolipid interactions.
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ISSN:0196-9781
1873-5169
DOI:10.1016/S0196-9781(01)00432-6