Evidence for an extended interacting surface between β-amyloid and serum amyloid P component

István Likó, Marianna Mák, E. Klement, E. Hunyadi-Gulyás, Tamás Pázmány, Katalin F. Medzihradszky, Zoltán Urbányi

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Studying the interaction between serum amyloid P component (SAP) and β-amyloid (Aβ) a new Aβ binding site was identified on the SAP near the known binding site at the two bound calcium ions. SAP stabilizes deposits in neurodegenerative diseases, which is manifested via Aβ-binding. Because the inhibition of this interaction is a potential therapeutic target in neurodegeneration, the structural basis of SAP-Aβ binding was studied. The chymotryptic digestion of SAP resulted in a 18,223 Da product identified by mass spectrometry. This cleavage was inhibited by Aβ revealing that this cleaving site between Tyr-140 and Gly-141 is involved in the interaction between SAP and Aβṡ These results suggest that the Aβ-binding site on SAP is larger than it was recently assumed.

Original languageEnglish
Pages (from-to)51-55
Number of pages5
JournalNeuroscience Letters
Volume412
Issue number1
DOIs
Publication statusPublished - Jan 22 2007

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Serum Amyloid P-Component
Amyloid
Binding Sites
Neurodegenerative Diseases
Digestion
Mass Spectrometry
Ions
Calcium

Keywords

  • β-Amyloid
  • Alzheimer's disease
  • Limited proteolysis
  • Mass spectrometry
  • Serum amyloid P component
  • Structural study

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Evidence for an extended interacting surface between β-amyloid and serum amyloid P component. / Likó, István; Mák, Marianna; Klement, E.; Hunyadi-Gulyás, E.; Pázmány, Tamás; Medzihradszky, Katalin F.; Urbányi, Zoltán.

In: Neuroscience Letters, Vol. 412, No. 1, 22.01.2007, p. 51-55.

Research output: Contribution to journalArticle

Likó, István ; Mák, Marianna ; Klement, E. ; Hunyadi-Gulyás, E. ; Pázmány, Tamás ; Medzihradszky, Katalin F. ; Urbányi, Zoltán. / Evidence for an extended interacting surface between β-amyloid and serum amyloid P component. In: Neuroscience Letters. 2007 ; Vol. 412, No. 1. pp. 51-55.
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