Structural analysis of amyloid ? peptide fragment (25-35) in different microenvironments

Biopolymers ◽  
2004 ◽  
Vol 76 (5) ◽  
pp. 421-434 ◽  
Author(s):  
Ganesh Shanmugam ◽  
Rajadas Jayakumar
Keyword(s):  
Structural Analysis ◽  
Amyloid Peptide ◽  
Peptide Fragment

The molecular mechanism of fullerene-inhibited aggregation of Alzheimer's β-amyloid peptide fragment

Nanoscale ◽  
2014 ◽  
Vol 6 (16) ◽  
pp. 9752-9762 ◽  
Author(s):  
Luogang Xie ◽  
Yin Luo ◽  
Dongdong Lin ◽  
Wenhui Xi ◽  
Xinju Yang ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Inhibitory Effect ◽  
Amyloid Peptide ◽  
Peptide Fragment ◽  
Experiment Study ◽  
Simulation And Experiment ◽  
Β Amyloid ◽  
Combined Simulation ◽  
Β Amyloid Peptide ◽  
Β Sheet

A combined simulation and experiment study demonstrates that fullerenes inhibit the β-sheet formation of Aβ(16–22) and fullerene hexagonal rings play a significant role on the inhibitory effect.

β-amyloid peptide fragment 31–35 induces apoptosis in cultured cortical neurons

Neuroscience ◽  
1999 ◽  
Vol 92 (1) ◽  
pp. 177-184 ◽  
Author(s):  
X.-Z Yan ◽  
J.-T Qiao ◽  
Y Dou ◽  
Z.-D Qiao
Keyword(s):  
Cortical Neurons ◽  
Amyloid Peptide ◽  
Peptide Fragment ◽  
Cultured Cortical Neurons ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Studies of the aggregation of an amyloidogenic α-synuclein peptide fragment

2005 ◽  
Vol 33 (5) ◽  
pp. 1113-1115 ◽  
Author(s):  
J. Madine ◽  
A.J. Doig ◽  
A. Kitmitto ◽  
D.A. Middleton
Keyword(s):  
Structural Analysis ◽  
Characteristic Feature ◽  
Neurodegenerative Disorders ◽  
Lewy Bodies ◽  
Structural Features ◽  
Full Length ◽  
Peptide Fragment ◽  
Structural Investigations ◽  
Detailed Structural Analysis ◽  
Β Sheet

The deposition of α-syn (α-synuclein) fibrils in Lewy bodies is a characteristic feature of individuals with neurodegenerative disorders. A peptide comprising the central residues 71–82 of α-syn [α-syn(71–82)] is capable of forming β-sheet-rich, amyloid-like fibrils with similar morphologies to fibrils of the full-length protein, providing a useful model of pathogenic α-syn fibrils that is suitable for detailed structural analysis. We have studied the morphology and gross structural features of α-syn(71–82) fibrils formed under different conditions in order to obtain reliable conditions for producing fibrils for further structural investigations. The results indicate that the rate of aggregation and the morphology of the fibrils formed are sensitive to pH and temperature.

scholarly journals Inhibition of Toxicity in the β-Amyloid Peptide Fragment β-(25–35) UsingN-Methylated Derivatives

2000 ◽  
Vol 275 (33) ◽  
pp. 25109-25115 ◽  
Author(s):  
Eleri Hughes ◽  
Ron M. Burke ◽  
Andrew J. Doig
Keyword(s):  
Amyloid Peptide ◽  
Peptide Fragment ◽  
Β Amyloid ◽  
Β Amyloid Peptide

Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization

2010 ◽  
Vol 1 (4) ◽  
pp. 453 ◽  
Author(s):  
V. Castelletto ◽  
G. E. Newby ◽  
D. Hermida Merino ◽  
I. W. Hamley ◽  
D. Liu ◽  
...  
Keyword(s):  
Phase Formation ◽  
Self Assembly ◽  
Amyloid Peptide ◽  
Peptide Fragment

Alignment of a Model Amyloid Peptide Fragment in Bulk and at a Solid Surface

2010 ◽  
Vol 114 (24) ◽  
pp. 8244-8254 ◽  
Author(s):  
Ian W. Hamley ◽  
Valeria Castelletto ◽  
Claire M. Moulton ◽  
José Rodríguez-Pérez ◽  
Adam M. Squires ◽  
...  
Keyword(s):  
Solid Surface ◽  
Amyloid Peptide ◽  
Peptide Fragment

Conformational Analysis of the β-amyloid Peptide Fragment, β(12–28)

1995 ◽  
Vol 13 (2) ◽  
pp. 229-244 ◽  
Author(s):  
Dimuthu Jayawickrama ◽  
Shana Zink ◽  
David Vander Velde ◽  
Rosemary I. Effiong ◽  
Cynthia K. Larive
Keyword(s):  
Conformational Analysis ◽  
Amyloid Peptide ◽  
Peptide Fragment ◽  
Β Amyloid ◽  
Β Amyloid Peptide
Sign in / Sign up

Export Citation Format

Share Document