Self-assembly of short amyloidogenic peptides at the air–water interface

Chaudhary, Nitin; Nagaraj, Ramakrishnan

doi:10.1016/j.jcis.2011.04.046

Cited by 11 publications

(13 citation statements)

References 50 publications

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“…The remarkable hysteresis observed in the case of PyA3UA is suggestive of irreversible changes caused by compression of the peptide film, probably due to formation of heterogeneous 3D aggregates. 35 Further differences are made evident by considering the variation of the surface compressibility modulus of the two compounds during formation of the peptide films. The surface compressibility factor (K) is defined as 1Basically, the higher the value of K, the tighter is the lateral packing of the molecules.…”

Section: Peptide Film Formation At the Air/water Interfacementioning

confidence: 99%

Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly

et al. 2018

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Peptide self-assembly is ubiquitous in nature. It governs the organization of proteins, controlling their folding kinetics and preserving their structural stability and bioactivity. In this connection, model oligopeptides may give important insights into the molecular mechanisms and elementary forces driving the formation of supramolecular structures. In this contribution, we show that a single residue substitution, that is, Aib (α-aminoisobutyric acid) in place of Ala at position 4 of an -(l-Ala)-homo-oligomer, strongly alters the aggregation process. In particular, this process is initiated by the formation of small peptide clusters that promote aggregation on the nanometer scale and, through a hierarchical self-assembly, lead to mesoscopic structures of micrometric dimensions. Furthermore, we show that the use of the well-established Langmuir-Blodgett technique represents an effective strategy for coating extended areas of inorganic substrates by densely packed peptide layers, thus paving the way for application of peptide films as templates for biomineralization, biocompatible coating of surfaces, and scaffolds for tissue engineering.

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Section: Peptide Film Formation At the Air/water Interfacementioning

confidence: 99%

Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly

et al. 2018

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“…These short peptides could self-assemble into typical amyloid fibrils on their own and played determinative roles for the amyloidogenic property of their full-length versions. [12][13][14][15][16][17][18][19] On the other hand, some de novo designed short peptides have also shown the ability to form amyloid fibrils, providing useful models for investigating the molecular basis of this intriguing process. [20][21][22][23][24][25] Although these peptides were still quite different from each other considering their exact amino acid sequences, a large proportion of them showed a common feature of amphiphilic structure, suggesting the essential role of hydrophobic interaction in the formation of amyloid fibrils.…”

Section: Introductionmentioning

confidence: 99%

Amyloid‐like aggregation of designer bolaamphiphilic peptides: Effect of hydrophobic section and hydrophilic heads

Qiu

Tang

Chen

2017

Journal of Peptide Science

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Amyloid-like aggregation of natural proteins or polypeptides is an important process involved in many human diseases as well as some normal biological functions. Plenty of works have been done on this ubiquitous phenomenon, but the molecular mechanism of amyloid-like aggregation has not been fully understood yet. In this study, we showed that a series of designer bolaamphiphilic peptides could undergo amyloid-like aggregation even though they didn't possess typical β-sheet secondary structure. Through systematic amino acid substitution, we found that for the self-assembling ability, the number and species of amino acid in hydrophobic section could be variable as long as enough hydrophobic interaction is provided, while different polar amino acids as the hydrophilic heads could change the self-assembling nanostructures with their aggregating behaviors affected by pH value change. Based on these results, novel self-assembling models and aggregating mechanisms were proposed, which might provide new insight into the molecular basis of amyloid-like aggregation.

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“…It was widely accepted that A β aggregates are generated by a nucleation-dependent polymerization mechanism, which is composed of two steps: the nucleation of A β peptides into short fibrils and the extension of the fibril ends by attachment with monomers [53]. In another work reported by Nagaraj et al, it has been shown that the AWI also influences the aggregation of shorter amyloidogenic peptides through enhanced self-assembly [54]. These works provide evidence that the AWI plays an essential role in the formation of A β -fibrils at a low concentration, in turn suggesting that the interference from the AWI should be carefully considered for a more precise evaluation of protein amyloidosis modulated by biological interfaces in vitro.…”

Section: Hydrophobic–hydrophilic Interfaces Triggered Accumulationmentioning

confidence: 99%

Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

et al. 2016

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Recently, studies of protein/peptide aggregation, particularly the amyloidosis, have attracted considerable attention in discussions of the pathological mechanisms of most neurodegenerative diseases. The protein/peptide aggregation processes often occur at the membrane–cytochylema interface in vivo and behave differently from those occurring in bulk solution, which raises great interest to investigate how the interfacial properties of artificial biomaterials impact on protein aggregation. From the perspective of bionics, current progress in this field has been obtained mainly from four aspects: (1) hydrophobic–hydrophilic interfaces; (2) charged surface; (3) chiral surface; and (4) biomolecule-related interfaces. The specific physical and chemical environment provided by these interfaces is reported to strongly affect the adsorption of proteins, transition of protein conformation, and diffusion of proteins on the biointerface, all of which are ultimately related to protein assembly. Meanwhile, these compelling results of in vitro experiments can greatly promote the development of early diagnostics and therapeutics for the relevant neurodegenerative diseases. This paper presents a brief review of these appealing studies, and particular interests are placed on weak interactions (i.e., hydrogen bonding and stereoselective interactions) that are also non-negligible in driving amyloid aggregation at the interfaces. Moreover, this paper also proposes the future perspectives, including the great opportunities and challenges in this field as well.

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Self-assembly of short amyloidogenic peptides at the air–water interface

Cited by 11 publications

References 50 publications

Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly

Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly

Amyloid‐like aggregation of designer bolaamphiphilic peptides: Effect of hydrophobic section and hydrophilic heads

Protein/Peptide Aggregation and Amyloidosis on Biointerfaces

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