Self-assembly of ionic-complementary peptides: a physicochemical viewpoint

Chen, P.

doi:10.1016/j.colsurfa.2004.12.048

Cited by 127 publications

(101 citation statements)

References 141 publications

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“…[41,42] Zhang and coworkers studied the aggregation of ionic complementary peptides comprising alternating hydrophobic and hydrophilic residues and differentiated between fibrillar or globular aggregate structures. [43,44] With the exception of the work by Lynn and coworkers these studies have not focused on a pHinduced morphology change of b-sheet-based aggregates, which is one aspect of the work we present here. Differences in the morphology of amyloid peptide fibrils can lead to differences in neurotoxicity, [45] and propagation of the fibrils, [45] as well as distinct phenotypes resulting from the mode of the self-assembly.…”

Section: Resultsmentioning

confidence: 50%

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

Hamley

Castelletto

Moulton

et al. 2009

Macromolecular Bioscience

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The self-assembly of peptide YYKLVFFC based on a fragment of the amyloid beta (A beta) peptide, A beta 16-20, KLVFF has been studied in aqueous solution. The peptide is designed with multiple functional residues to examine the interplay between aromatic interactions and charge on the self-assembly, as well as specific transformations such as the pH-induced phenol-phenolate transition of the tyrosine residue. Circular dichroism (CD) and Fourier-transform infrared (FTIR) spectroscopies are used to investigate the conditions for beta-sheet self-assembly and the role of aromatic interactions in the CD spectrum as a function of pH and concentration. The formation of well-defined fibrils at pH 4.7 is confirmed by cryo-TEM (transmission electron microscope) and negative stain TEM. The morphology changes at higher pH, and aggregates of short twisted fibrils are observed at pH 11. Polarized optical microscopy shows birefringence at a low concentration (1 wt.-%) of YYKLVFFC in aqueous solution, and small-angle X-ray scattering was used to probe nematic phase formation in more detail. A pH-induced transition from nematic to isotropic phases is observed on increasing pH that appears to be correlated to a reduction in aggregate anisotropy upon increasing pH.

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Section: Resultsmentioning

confidence: 50%

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

Hamley

Castelletto

Moulton

et al. 2009

Macromolecular Bioscience

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“…The process of self-assembly is based on spontaneous organization of molecules through smart recognition. This process is often governed by noncovalent interactions, such as electrostatic, hydrophobic, metal-ligand interactions and van der Waals forces, hydrogen bond formation and aromatic π-stacking [2,3]. Although these interactions are rather weak individually, when sufficient in number they can govern the structural conformation and generate stable assemblies.…”

Section: Introductionmentioning

confidence: 99%

Constructing biomaterials using self-assembling peptide building blocks

Chen

2010

Front. Mater. Sci. China

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Molecular self-assembly is ubiquitous in nature and has recently emerged as a new bottom-up approach in constructing biomaterials. Synthetic peptides assemble through specific molecular recognition and form diverse nanostructures. The resulting versatile peptide selfassemblies may be used in a wide range of biological and medical applications. Examples of two self-assembling peptide systems are presented and techniques for selfassembly control are discussed.

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“…The most common of these is simply increasing the concentration of peptide, which increases the number, or length, of the fibrillar structures present and in turn leads to an increase in entanglements in the system. 13,14 More subtle methods include varying the amino acid sequence, where the inclusion of more hydrophobic amino acids increases the attraction between individual fibers. 15 The same effect can be gained by varying media pH or through the addition of salt when charged amino acids are present.…”

Section: Introductionmentioning

confidence: 99%

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

2014

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Oligopeptides are well-known to self-assemble into a wide array of nanostructures including β-sheet-rich fibers that when present above a critical concentration become entangled and form self-supporting hydrogels. The length, quantity, and interactions between fibers influence the mechanical properties of the hydrogel formed and this is typically achieved by varying the peptide concentration, pH, ionic strength, or the addition of a second species or chemical cross-linking agent. Here, we outline an alternative, facile route to control the mechanical properties of the self-assembling octa-peptide, FEFEFKFK (FEKII); simply doping with controlled quantities of its double length peptide, FEFEFKFK-GG-FKFKFEFE (FEKII18). The structure and properties of a series of samples were studied here (0–100 M% of FEKII18) using Fourier transform infrared, small angle X-ray scattering, transmission electron microscopy, and oscillatory rheology. All samples were found to contain elongated, flexible fibers and all mixed samples contained Y-shaped branch points and parallel fibers which is attributed to the longer peptide self-assembling within two fibers, thus creating a cross-link in the network structure. Such behavior was reflected in an increase in the elasticity of the mixed samples with increasing quantity of double peptide. Interestingly the elastic modulus increased up to 30 times the pure FEKII value simply by adding 28 M% of FEKII18. These observations provide an easy, off-the-shelf method for an end-user to control the cross-linked network structure of the peptide hydrogel, and consequently strength of the hydrogel simply by physically mixing pre-determined quantities of two similar peptide molecules.

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Self-assembly of ionic-complementary peptides: a physicochemical viewpoint

Cited by 127 publications

References 141 publications

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

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

Constructing biomaterials using self-assembling peptide building blocks

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

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