Conformational mapping of amyloid peptides from the putative neurotoxic 25-35 region.
Biochem Biophys Res Commun
; 205(1): 120-6, 1994 Nov 30.
Article
em En
| MEDLINE
| ID: mdl-7999011
ABSTRACT
The secondary structure of amyloid beta A(25-35) and its deletion analogues was studied by circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy and molecular dynamics calculation. Data of our comparative CD and FTIR measurements in trifluoroethanol suggest that beta A(25-35)NH2 has a preferred beta-sheet conformation. Contrary to this beta A(31-35)NH2 tends to adopt a beta-turn conformation. Based on the comparable neurotoxic effect of beta A(25-35)NH2 and beta A(31-35)NH2 the neurotoxicity likely involves the same 31-35 core sequence and the "biologically active conformation" is a beta-turn rather than a beta-sheet structure.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Peptídeos beta-Amiloides
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1994
Tipo de documento:
Article