Volume 123, Issue 46 pp. 11051-11054
Zuschrift

A Membrane-Bound Antiparallel Dimer of Rat Islet Amyloid Polypeptide

Dr. Abhinav Nath

Dr. Abhinav Nath

Molecular Biophysics & Biochemistry, Yale University, New Haven CT 06520-8114 (USA)

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Prof. Andrew D. Miranker

Corresponding Author

Prof. Andrew D. Miranker

Molecular Biophysics & Biochemistry, Yale University, New Haven CT 06520-8114 (USA)

Molecular Biophysics & Biochemistry, Yale University, New Haven CT 06520-8114 (USA)Search for more papers by this author
Prof. Elizabeth Rhoades

Corresponding Author

Prof. Elizabeth Rhoades

Molecular Biophysics & Biochemistry, Yale University, New Haven CT 06520-8114 (USA)

Molecular Biophysics & Biochemistry, Yale University, New Haven CT 06520-8114 (USA)Search for more papers by this author
First published: 22 September 2011
Citations: 4

This work was funded by an American Heart Association Postdoctoral Fellowship for A.N. and NIH grant GM-084391 to E.R. and A.D.M. We thank Dr. S. G. Sligar (UIUC) for the gift of MSP1D1, Y. Gofman of the Ben-Tal group (Tel Aviv University) for assistance with MCPep, Dr. J. Knight, Dr. T. Craggs, and Dr. C. J. Wilson for critical reading, J. Dunn for expressed IAPP, the W. M. Keck Biotechnology Research Laboratory for peptide synthesis, and the Yale FAS High Performance Computing Center.

Graphical Abstract

Aufschlussreich: Die Struktur eines antiparallelen Dimers des Inselamyloidpolypeptids der Ratte im Komplex mit anionischen Membrannanoscheibchen wurde durch Einzelpaar(sp)-FRET und Rosetta-Verfeinerung untersucht. Modelle des Dimers offenbarten eine mögliche Schnittstelle für die Lipidbindung und lassen vermuten, dass wesentliche Wechselwirkungen auch in der humanen Isoform auftreten. Die Befunde könnten Einblicke in die Fibrillenbildung bei Diabetes Typ II geben.

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