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Aggregation of Aβ(1–42) in the presence of short peptides: conformational studies
Author(s) -
Laczkó Ilona,
Vass Elemér,
Soós Katalin,
Fülöp Livia,
Zarándi Márta,
Penke Botond
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.990
Subject(s) - fibrillogenesis , chemistry , peptide , inhibitory postsynaptic potential , fibril , stereochemistry , biophysics , biochemistry , medicine , biology
CD and infrared spectroscopic studies were performed on (i) the inhibitory effects of equimolar quantities of LPFFD‐OH and LPYFD‐NH 2 on the time‐dependent aggregation of amyloid β‐protein (Aβ) (1–42) and (ii) the β‐sheet‐breaker effects of two‐fold molar excess of the pentapeptides on aggregated Aβ(1–42) aged 1 week. The data obtained from the time‐dependent studies demonstrated that LPFFD‐OH did not significantly influence, whereas LPYFD‐NH 2 exerted some inhibitory effect on the aggregation of Aβ(1–42). When added to a solution of Aβ(1–42) aged 1 week, LPFFD‐OH accelerated, while LPYFD‐NH 2 delayed, but did not prevent further fibrillogenesis. The difference in the effects of these two pentapeptides on the aggregational profile of Aβ(1–42) is probably due to the difference in their conformational preferences: LPFFD‐OH adopts a β‐turn and extended structures, while LPYFD‐NH 2 adopts a prevailing β‐turn conformation. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.