Role of Aromatic Interactions in Amyloid Formation by Peptides Derived from Human Amylin†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15901-15908 ◽  
Author(s):  
Sylvia M. Tracz ◽  
Andisheh Abedini ◽  
Miles Driscoll ◽  
Daniel P. Raleigh
2019 ◽  
Vol 32 (2) ◽  
pp. 87-93 ◽  
Author(s):  
Kyung-Hoon Lee ◽  
Alexander Zhyvoloup ◽  
Daniel Raleigh

Abstract The polypeptide amylin is responsible for islet amyloid in type 2 diabetes, a process which contributes to β-cell death in the disease. The role of the N-terminal region of amylin in amyloid formation is relatively unexplored, although removal of the disulfide bridged loop between Cys-2 and Cys-7 accelerates amyloid formation. We examine the des Lys-1 variant of human amylin (h-amylin), a variant which is likely produced in vivo. Lys-1 is a region of high charge density in the h-amylin amyloid fiber. The des Lys-1 polypeptide forms amyloid on the same time scale as wild-type amylin in phosphate buffered saline, but does so more rapidly in Tris. The des Lys-1 variant is somewhat less toxic to cultured INS cells than wild type. The implications for the in vitro mechanism of amyloid formation and for comparative analysis of amyloidogenicity are discussed.


2010 ◽  
Vol 114 (12) ◽  
pp. 4313-4324 ◽  
Author(s):  
R. Mahesh Kumar ◽  
M. Elango ◽  
V. Subramanian

2014 ◽  
Vol 106 (7) ◽  
pp. 1520-1527 ◽  
Author(s):  
Ling-Hsien Tu ◽  
Arnaldo L. Serrano ◽  
Martin T. Zanni ◽  
Daniel P. Raleigh

Biochemistry ◽  
2013 ◽  
Vol 52 (49) ◽  
pp. 8800-8810 ◽  
Author(s):  
Narendra Nath Jha ◽  
A. Anoop ◽  
Srivastav Ranganathan ◽  
Ganesh M. Mohite ◽  
Ranjith Padinhateeri ◽  
...  
Keyword(s):  

2010 ◽  
pp. 615-630 ◽  
Author(s):  
Johanna C. Scheinost ◽  
Daniel P. Witter ◽  
Grant E. Boldt ◽  
Paul Wentworth

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