Self-Assembly and Hydrogelation of an Amyloid Peptide Fragment

Biochemistry ◽  
2008 ◽  
Vol 47 (16) ◽  
pp. 4597-4605 ◽  
Author(s):  
Marta J. Krysmann ◽  
Valeria Castelletto ◽  
Antonios Kelarakis ◽  
Ian W. Hamley ◽  
Rohan A. Hule ◽  
...  
Keyword(s):  
Self Assembly ◽  
Amyloid Peptide ◽  
Peptide Fragment

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

Self-Assembly of a Modified Amyloid Peptide Fragment: pH-Responsiveness and Nematic Phase Formation

2010 ◽  
Vol 10 (1) ◽  
pp. 40-48 ◽  
Author(s):  
Ian W. Hamley ◽  
Valeria Castelletto ◽  
Claire Moulton ◽  
Daniel Myatt ◽  
Giuliano Siligardi ◽  
...  
Keyword(s):  
Phase Formation ◽  
Self Assembly ◽  
Nematic Phase ◽  
Amyloid Peptide ◽  
Peptide Fragment

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

scholarly journals Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm.

1986 ◽  
Vol 103 (5) ◽  
pp. 1689-1697 ◽  
Author(s):  
A S Charonis ◽  
E C Tsilibary ◽  
T Saku ◽  
H Furthmayr
Keyword(s):  
Self Assembly ◽  
Binding Sites ◽  
Type Iv Collagen ◽  
Specific Interaction ◽  
Basement Membranes ◽  
Complex Domain ◽  
Peptide Fragment ◽  
Type Iv ◽  
Collagen Molecules

Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross-shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.

scholarly journals Melanin production by tyrosinase activity on a tyrosine-rich peptide fragment and pH-dependent self-assembly of its lipidated analogue

2019 ◽  
Vol 17 (18) ◽  
pp. 4543-4553 ◽  
Author(s):  
Jessica A. Hutchinson ◽  
Ian W. Hamley ◽  
Charlotte J. C. Edwards-Gayle ◽  
Valeria Castelletto ◽  
Cristian Piras ◽  
...  
Keyword(s):  
Self Assembly ◽  
Tyrosinase Activity ◽  
The Self ◽  
Peptide Fragment ◽  
Melanin Production ◽  
Gut Hormone ◽  
Ph Dependent

The self-assembly of a palmitoylated peptide C16-EELNRYY based on a fragment of the gut hormone peptide PYY3–36 is investigated.

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.

Manipulation of self-assembly amyloid peptide nanotubes by dielectrophoresis

2008 ◽  
Vol 29 (24) ◽  
pp. 5026-5032 ◽  
Author(s):  
Jaime Castillo ◽  
Simone Tanzi ◽  
Maria Dimaki ◽  
Winnie Svendsen
Keyword(s):  
Self Assembly ◽  
Amyloid Peptide ◽  
Peptide Nanotubes
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