Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
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Self-assembling amphiphilic peptidesDynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide.Probing droplets on superhydrophobic surfaces by synchrotron radiation scattering techniques.Tetrapeptidic molecular hydrogels: self-assembly and co-aggregation with amyloid fragment Aβ1-40.Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides.Structural and optical properties of short peptides: nanotubes-to-nanofibers phase transformation.De novo design and experimental characterization of ultrashort self-associating peptidesSupramolecular amplification of amyloid self-assembly by iodination.The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies.Amyloid-based nanosensors and nanodevices.Growth-incompetent monomers of human calcitonin lead to a non-canonical direct relationship between peptide concentration and lag time.Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids.Aggregation gatekeeper and controlled assembly of Trpzip β-hairpinsSelf-assembling peptide-based building blocks in medical applications.Peptides conjugated to silver nanoparticles in biomedicine - a "value-added" phenomenon.Superhydrophobic surfaces allow probing of exosome self organization using X-ray scattering.Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils.Systematic Moiety Variations of Ultrashort Peptides Produce Profound Effects on Self-Assembly, Nanostructure Formation, Hydrogelation, and Phase Transition.Two-step kinetic model of the self-assembly mechanism for diphenylalanine micro/nanotube formation.The Physiological and Pathological Implications of the Formation of Hydrogels, with a Specific Focus on Amyloid Polypeptides.Crystallographic insights into the self-assembly of KLVFF amyloid-beta peptides.A short non-cytotoxic antimicrobial peptide designed from Aβ29-40 adopts a nanostructure and shows in vivo anti-endotoxin activity.Molecular simulations of peptide amphiphiles.Tunable Pentapeptide Self-Assembled β-Sheet Hydrogels.Molecular simulations of self-assembling bio-inspired supramolecular systems and their connection to experiments.A dimer model of human calcitonin13-32 forms an α-helical structure and robustly aggregates in 50% aqueous 2,2,2-trifluoroethanol solution.Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptideThe interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide
P2860
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P2860
Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@ast
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@en
type
label
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@ast
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@en
prefLabel
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@ast
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@en
P2093
P2860
P50
P356
P1476
Aliphatic peptides show simila ...... ic interactions in amyloidosis
@en
P2093
Christian Riekel
Daniel W Cheong
Enzo Di Fabrizio
P2860
P304
P356
10.1073/PNAS.1217742110
P407
P577
2012-12-24T00:00:00Z