Self-assembly in aqueous solution of a modified amyloid beta peptide fragment

Castelletto, Valeria; Hamley, Ian W.; Harris, Peter

doi:10.1016/j.bpc.2008.08.007

Cited by 51 publications

(79 citation statements)

References 24 publications

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“…This 225 nm minimum is red-shifted compared to the characteristic β-sheet minimum near 217 nm (ref. 55), yet similar spectra were previously reported in other supramolecular β-sheet peptide assemblies5657. Lastly, ThT binding further supported the formation of β-sheets by the 9-mer (Fig.…”

Section: Resultssupporting

confidence: 87%

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

et al. 2016

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Mimicking the multifunctional bacterial type IV pili (T4Ps) nanofibres provides an important avenue towards the development of new functional nanostructured biomaterials. Yet, the development of T4Ps-based applications is limited by the inability to form these nanofibres in vitro from their pilin monomers. Here, to overcome this limitation, we followed a reductionist approach and designed a self-assembling pilin-based 20-mer peptide, derived from the presumably bioelectronic pilin of Geobacter sulfurreducens. The designed 20-mer, which spans sequences from both the polymerization domain and the functionality region of the pilin, self-assembled into ordered nanofibres. Investigation of the 20-mer revealed that shorter sequences which correspond to the polymerization domain form a supramolecular β-sheet, contrary to their helical configuration in the native T4P core, due to alternative molecular recognition. In contrast, the sequence derived from the functionality region maintains a native-like, helical conformation. This study presents a new family of self-assembling peptides which form T4P-like nanostructures.

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Section: Resultssupporting

confidence: 87%

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

et al. 2016

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“…The FT-IR spectrum of Boc-II-OMe ( Figure 6A) shows bands at 1625 and 1682 cm À1 , suggesting the presence of antiparallel b-sheet conformation [48][49][50][51][52][53][54][55]. An additional band at 1648 cm À1 suggests the presence of unordered structure [48,55].…”

Section: Attenuated Total Internal Reflection Ft-ir Spectroscopymentioning

confidence: 99%

Self‐assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids

Subbalakshmi

Manorama

Nagaraj

2012

Journal of Peptide Science

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The morphology of structures formed by the self-assembly of short N-terminal t-butyloxycarbonyl (Boc) and C-terminal methyl ester (OMe) protected and Boc-deprotected hydrophobic peptide esters was investigated. We have observed that Boc-protected peptide esters composed of either only aliphatic hydrophobic amino acids or aliphatic hydrophobic amino acids in combination with aromatic amino acids, formed highly organized structures, when dried from methanol solutions. Transmission and scanning electron microscopic images of the peptides Boc-Ile-Ile-OMe, Boc-Phe-Phe-Phe-Ile-Ile-OMe and Boc-Trp-Ile-Ile-OMe showed nanotubular structures. Removal of the Boc group resulted in disruption of the ability to form tubular structures though spherical aggregates were formed. Both Boc-Leu-Ile-Ile-OMe and H-Leu-Ile-Ile-OMe formed only spherical nanostructures. Dynamic light scattering studies showed that aggregates of varying dimensions were present in solution suggesting that self-assembly into ordered structures is facilitated by aggregation in solution. Fourier transform infrared spectroscopy and circular dichroism spectroscopy data show that although all four of the protected peptides adopt well-defined tertiary structures, upon removal of the Boc group, only H-Phe-Phe-Phe-Ile-Ile-OMe had the ability to adopt β-structure. Our results indicate that hydrophobic interaction is a very important determinant for self-assembly and presence of charged and aromatic amino acids in a peptide is not necessary for self-assembly.

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“…The values of 4.8 Å and 12.6 Å are similar to those seen in fibrillar protein aggregates, such as Aβ plaques. 13 Previous work has indicated that the 4.8 Å peak likely belongs to the hydrogen bonding distance in the β-sheet, whereas the 12.6 Å peak is attributed to the spacing between β-sheets. 7 In contrast, PA 2 showed no significant diffraction in either the freshly dissolved solution or any of the aged solutions (Figure S6).…”

mentioning

confidence: 96%

“…Efforts to find the minimum peptide segment necessary for Aβ protein fibrillization have yielded the KLVFF sequence. 7,13,14 Phenylalanine residues are of particular importance in the aggregation of Aβ. 15 In this context, Gazit et al demonstrated that only a dimer of phenylalanine is needed to assemble into nanotubes as a result of the π-π stacking.…”

mentioning

confidence: 99%

Direct Observation of Morphological Tranformation from Twisted Ribbons into Helical Ribbons

2010

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We report on the direct observation of a nanostructural transformation from a twisted ribbon to a helical ribbon in supramolecular assemblies of peptide amphiphiles. Using cryogenic electron microscopy, a peptide amphiphile molecule containing aromatic residues was found to first assemble into short twisted ribbons in the time range of seconds, which then elongate in the time scale of minutes, and finally transform into helical ribbons over the course of weeks. By synthesizing an analogous molecule without the aromatic side groups, it was found that a cylindrical nanostructure is formed that does not undergo any transitions during the same time period. The study of metastable states in peptide aggregation can contribute to our understanding of amyloid-related diseases such as Alzheimer’s.

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Self-assembly in aqueous solution of a modified amyloid beta peptide fragment

Cited by 51 publications

References 24 publications

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

Self‐assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids

Direct Observation of Morphological Tranformation from Twisted Ribbons into Helical Ribbons

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