The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution.

  title={The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution.},
  author={Penchit Chitnumsub and Wayne R. Fiori and Hilal A. Lashuel and Humberto Gonz{\'a}lez D{\'i}az and Jeffery W. Kelly},
  journal={Bioorganic \& medicinal chemistry},
  volume={7 1},
Ion Pairing Between the Chain Ends Induces Folding of a Flexible Zwitterion in Methanol
A well defined folded loop structure can be induced in a flexible zwitterion 10 in the polar and protic solvent methanol by charge interactions between the two termini of the zwitterion. In 10 a
Impact of strand length on the stability of parallel-β-sheet secondary structure.
Novel strategies are required to elucidate the factors that govern parallel-β-sheet stability, including introducing significant tertiary packing effects or an entropic penalty for folding, either of which would compromise the analysis.
The synthesis and study of side-chain lactam-bridged peptides.
Defining the functional roles of the amphiphilic alpha-helices in medium-sized peptide hormones, and studying helix propagation from rigid, alpha-helix initiating bicyclic peptides are among the most exciting developments currently underway in this field.
Impact of Strand Number on Parallel β-Sheet Stability.
Analysis of the designed peptides by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of β-strands, from two to three, increases the stability of the parallel β-sheet.
New cylindrical peptide assemblies defined by extended parallel β-sheets.
A new approach to non-covalent peptide-based nanotubular or rod-like structures is presented, whereby the monomeric units are preorganised into a β-strand geometry that templates the formation of an
Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Aβ1–40 fibrillogenesis
It is demonstrated, through two-dimensional NMR and circular dichroic spectroscopy, that a pentapeptide with two N-methyl amino acids, Abeta16-20m or Ac-K(me)LV(Me)FF-NH2, does indeed have the intended structure of an extended beta-strand and is able to pass spontaneously through both synthetic phospholipid bilayer vesicles and cell membranes.
A Comparative Study on the Self-Assembly of Peptide TGV-9 by In Situ Atomic Force Microscopy
Investigation of the self-assembling of a Parkinson disease-related core peptide sequence (TGV-9) on a hydrophobic liquid–solid interface via real-time observation of the dynamic fibrillization process shows an epitaxial growth or TASA, which could not only deepen the understanding of the protein/peptide aggregation mechanism but also benefit for the early diagnosis and clinic treatment of related diseases.
Prevention of Alzheimer's Disease-associated Aβ Aggregation by Rationally Designed Nonpeptidic β-Sheet Ligands*
It is concluded that these β-sheet ligands do not prevent the initial oligomerization of monomeric Aβ but rather block further aggregation of spontaneously formed small oligomers.


Nucleated Antiparallel β-Sheet That Folds and Undergoes Self-Assembly: A Template Promoted Folding Strategy toward Controlled Molecular Architectures
The approach described here takes advantage of template driven hydrophobic clusters and template derived conformational biases to nucleate folding in small peptides, affording β-sheets which subsequently self-associate into fibrils.
This paper describes the solid-phase syntheses of artificial β-sheets 1−4, which mimic the structure and hydrogen-bonding patterns of protein β-sheets. In these compounds, molecular templates induce
A 2,3‘-Substituted Biphenyl-Based Amino Acid Facilitates the Formation of a Monomeric β-Hairpin-like Structure in Aqueous Solution at Elevated Temperature
An NMR structural evaluation of heptapeptides incorporating 1 revealed the presence of a hydrophobic cluster involving an aromatic ring of 1 and a side chain of one of the flankingHydrophobic α-amino acids, even though the peptides lack sufficient length to adopt a β-sheet structure.
Measurement of the β-sheet-forming propensities of amino acids
The relative propensity for β-sheet formation of the twenty naturally occurring amino acids in a variant of the small, monomeric,β-sheet-rich, IgG-binding domain from protein G is measured.
Use of a Designed Triple-Stranded Antiparallel β-Sheet To Probe β-Sheet Cooperativity in Aqueous Solution
Cooperativity is a defining characteristic of protein tertiary structure; partially folded forms are usually less stable than either the native conformation or the denatured state. 1 Cooperativity
Thermodynamic β -sheet propensities measured using a zinc-finger host peptide
A thermodynamic β -sheet propensity scale for all the commonly occurring amino acids in aqueous solution is presented and the relative free energies correlate well with previously derived potential values based on statistical analysis of protein structures.
A Modular Approach to Polymer Architecture Control via Catenation of Prefabricated Biomolecular Segments: Polymers Containing Parallel β-Sheets Templated by a Phenoxathiin-Based Reverse Turn Mimic
A biomolecular Lego set modular method whereby prefabricated building blocks are linked block by block has been developed and applied to the synthesis of peptide-based polymers containing parallel
Context is a major determinant of β-sheet propensity
RESIDUES in β-sheets occur in two distinct tertiary contexts: central strands, bordered on both sides by other β-strands, and edge strands, bordered on only a single side by another β-strand1. The
Cooperative Interaction between the Three Strands of a Designed Antiparallel β-Sheet
We describe the de novo design and characterization of a three stranded antiparallel β-sheet (peptide 1−24) and investigate the interplay between the two sets of weak interactions that occur at the
Mechanism of Stabilization of Helical Conformations of Polypeptides by Water Containing Trifluoroethanol
In dilute aqueous solution TFE increases helicity by selectively destabilizing amide functions that are solvent exposed, with the consequence that compact conformations such as helices that maximize intramolecular amide−amide hydrogen bonding and minimize amide solvent exposure are selectively favored.