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Cross‐Amyloid Interaction of Aβ and IAPP at Lipid Membranes
Author(s) -
Seeliger Janine,
Evers Florian,
Jeworrek Christoph,
Kapoor Shobhna,
Weise Katrin,
Andreetto Erika,
Tolan Metin,
Kapurniotu Aphrodite,
Winter Roland
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201105877
Subject(s) - amyloid (mycology) , membrane , chemistry , islet , raft , biochemistry , biophysics , biology , organic chemistry , copolymer , polymer , insulin , endocrinology , inorganic chemistry
Membrane controlled protein assembly : A study of the amyloid interaction of the islet amyloid polypeptide (IAPP), β‐amyloid (Aβ), and a mixture of both with an anionic model raft membrane showed the dominant effect of IAPP on the aggregation process and on the hydrogen‐bonding pattern of the assemblies present in the mixture (see picture). The analysis of the interaction of Aβ with IAPP‐GI—a non‐amyloidogenic IAPP mimic—confirmed these findings.