Peptidic self-assembled nanostructures are said to have a wide range of applications in nanotechnology, yet the mechanistic details of hierarchical self-assembly are still poorly understood. The Phe-Phe recognition motif of the Alzheimer's Abeta peptide is the smallest peptide able to assemble into higher-order structures. Here, we show that the Ile-Phe dipeptide analog is also able to self-associate in aqueous solution as a transparent, thermoreversible gel formed by a network of fibrillar nanostructures that exhibit strong birefringence upon Congo red binding. Besides, a second dipeptide Val-Phe, differing only in a methyl group from the former, is unable to self-assemble. The detailed analysis of the differential polymeric behavior of these closely related molecules provides insight into the forces triggering the first steps in self-assembly processes such as amyloid formation.
Ile-phe dipeptide self-assembly: clues to amyloid formation. Publishing Authors By Initials
Ile-phe dipeptide self-assembly: clues to amyloid formation. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Biophysical journal
VOLUME: 92
Page Numbers: 1732-41
Journal Abbreviation: Biophys. J.
ISSN: 0006-3495
DAY: 15
MONTH: 12
YEAR: 2006
Ile-phe dipeptide self-assembly: clues to amyloid formation. Information
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LANGUAGE: eng
NlmUniqueID: 370626
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Grant and Affiliation Information for Ile-phe dipeptide self-assembly: clues to amyloid formation.
AFFILIATION: Departament de Bioquímica i Biologia Molecular, Servei de Ressonància Magnètica Nuclear, and Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra (Barcelona), Spain.
Country: United States
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MEDLINETA: Biophys J
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