Use this url to cite publication: https://hdl.handle.net/20.500.12512/57356
Options
In-vitro fibril formation from alpha(1)-antitrypsin-derived c-terminal peptides / S. Janciauskiene, E. Carlemalm, S. Eriksson
Type of publication
Straipsnis Web of Science duomenų bazėje / Article in Web of Science database (S1a)
Author(s)
University Hospital Malmö, Malmö, Sweden | |
Carlhäll, Carljohan | Linköping University Hospital, Sweden |
Eriksson, Sten | Lund University, Department of Medicine, Malmo General Hospital, Sweden |
Title
In-vitro fibril formation from alpha(1)-antitrypsin-derived c-terminal peptides / S. Janciauskiene, E. Carlemalm, S. Eriksson
Extent
p. 415-423.
Is part of
Biological Chemistry Hoppe-Seyler. , 1995, vol. 376, no. 7.
Version
Originalus / Original
Field of Science
Keywords
Abstract
Fragments from various proteolytically degraded precursor proteins can form beta-amyloid fibrils. We studied, by electron microscopy and quantitative Congo red binding, the ability of three synthetic peptides, corresponding to residues 359-374 (C-36), 370-374 (C-5) and 375-394 (C-20) from the C-terminal part of alpha(1)-antitrypsin (AAT) to form beta-amyloid fibrils in vitro. The peptides C-36 and C-5 had a pronounced tendency to form fibrils. C-20 lacked this property, suggesting that residues 359-375 and/or 370-374 are most critical for fibril formation. Native AAT added to peptide I-125-C-36 could bind and form complexes with the peptide, resulting in inhibition of amyloid fibril formation. Moreover, native AAT added to preformed fibrils induced disaggregation of fibrillar structures. The structural rearrangements of AAT that occurred during this 'autointeraction' included polymerization of the serpin, and an increase of its thermal stability. Also, following interaction, an increase (20-40%) of AAT's antielastase activity was noted. The demonstration of an in vitro P-amyloid fibril formation from the AAT derived C-terminal peptides C-36 and C-5 and its regulation by the intact AAT molecule may have important in vivo implications.
Type of document
type::text::journal::journal article
ISSN (of the container)
0177-3593
WOS
A1995RL15300005
Other Identifier(s)
(LSMU ALMA)990000398620107106
Coverage Spatial
Jungtinės Amerikos Valstijos / United States of America (US)
Language
Anglų / English (en)