Neuropeptides interact with glycolipid receptors: a surface plasmon resonance study.

Abstract:

:Using Surface Plasmon Resonance (SPR) we investigated the interaction of seven neuropeptides with different characteristics and beta-amyloid (Abeta42) 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, Abeta42 > DYN > SP = GAL = SOM = BRD > OXY = ENK; for GD1a, Abeta42 = DYN = GAL > SP = SOM = BRD = OXY > ENK and for GT1b, Abeta42 > 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 Abeta42 and SP with gangliosides differed from the interactions of the other studied peptides. Ca(2+) promoted changes in peptide-glycolipid interactions.

journal_name

Peptides

journal_title

Peptides

authors

Valdes-Gonzalez T,Inagawa J,Ido T

doi

10.1016/s0196-9781(01)00432-6

subject

Has Abstract

pub_date

2001-07-01 00:00:00

pages

1099-106

issue

7

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(01)00432-6

journal_volume

22

pub_type

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