Neuropeptides interact with glycolipid receptors A surface plasmon resonance study

• Published in: Peptides (New York, N.Y. : 1980) Vol. 22; no. 7; pp. 1099 - 1106
• Main Authors: Valdes-Gonzalez, Tania, Inagawa, Junichi, Ido, Tatsuo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.07.2001
• Subjects: Amino Acid Sequence; asialo-GM1; Aβ42; Calcium - metabolism; Calcium - pharmacology; Calcium Chloride - pharmacology; Carbohydrate Sequence; G(M1) Ganglioside - metabolism; Gangliosides - chemistry; Gangliosides - metabolism; GD1a; Glycolipids - chemistry; GM1; GT1b; Kinetics; Molecular Sequence Data; neuropeptides; Neuropeptides - chemistry; Neuropeptides - metabolism; Peptides - chemistry; Peptides - metabolism; Protein Binding; Surface Plasmon Resonance; Surface Plasmon Resonance - methods; Time Factors; Surface Plasmon Resonance; Aβ42; neuropeptides; GM1; GD1a; asialo-GM1; Ca; GT1b
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/S0196-9781(01)00432-6

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.