Functional Peptide Monolayers at Interfaces

Leshem, Avigail Baruch; Zarzhitsky, Shlomo; Rapaport, Hanna

doi:10.1002/ijch.201400172

Cited by 4 publications

(2 citation statements)

References 60 publications

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“…Rapaport et al have reviewed the design and application of AP assemblies in monolayers at interfaces. 111 They also reported that acidic b-sheet peptides exhibited compressibility and elasticity, which may be associated with favorable cross-strand interactions between the side chains of peptides. 112 Recently, Bai and Ulijn et al successfully utilized nanofibrous interfacial networks assembled by amphiphilic peptides through p-stacking and hydrogen bonding interactions, to obtain a stable emulsion (Fig.…”

Section: The Kinetic Control Of Ap Self-assemblymentioning

confidence: 98%

Peptide self-assembly: thermodynamics and kinetics

et al. 2016

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Self-assembling systems play a significant role in physiological functions and have therefore attracted tremendous attention due to their great potential for applications in energy, biomedicine and nanotechnology. Peptides, consisting of amino acids, are among the most popular building blocks and programmable molecular motifs. Nanostructures and materials assembled using peptides exhibit important potential for green-life new technology and biomedical applications mostly because of their bio-friendliness and reversibility. The formation of these ordered nanostructures pertains to the synergistic effect of various intermolecular non-covalent interactions, including hydrogen-bonding, π-π stacking, electrostatic, hydrophobic, and van der Waals interactions. Therefore, the self-assembly process is mainly driven by thermodynamics; however, kinetics is also a critical factor in structural modulation and function integration. In this review, we focus on the influence of thermodynamic and kinetic factors on structural assembly and regulation based on different types of peptide building blocks, including aromatic dipeptides, amphiphilic peptides, polypeptides, and amyloid-relevant peptides.

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Section: The Kinetic Control Of Ap Self-assemblymentioning

confidence: 98%

Peptide self-assembly: thermodynamics and kinetics

et al. 2016

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“…Self-assembling peptides have been identified as candidates that can serve as building blocks in the fabrication of molecular devices: potential applications based on their ease of synthesis, ease and range of accessible chemical modification, and geometrical precision have been discussed in a number of reviews. − Recently, for example, advances have been made in the exploration of self-assembling peptides for applications such as drug delivery, organic semiconductor devices, and sensing . There has been significant progress in creating functional supramolecular structures using the Langmuir–Blodgett (LB) technique.…”

Section: Introductionmentioning

confidence: 99%

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

et al. 2020

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We demonstrate the assembly of a compact, gel-like Langmuir−Blodgett film of rods formed by self-assembly of a βsheet-forming water-soluble peptide, Ac-IKHLSVN-NH 2 , at the surface of aqueous electrolytes. We characterize surface pressure hysteresis and demonstrate shear stiffening of the surface caused by area cycling, which we interpret as due to rearrangement and alignment of the rods. We show strong effects of the electrolyte on the assembly of the elementary rods, which can be related to the Hofmeister series and interpreted by effects on the interaction energies mediated by ions and water. Formation of β-sheet structures and assembly of these into surface-segregated semicrystalline gels was strongly promoted by ammonium sulfate electrolyte. With ammonium sulfate electrolyte as subphase for Langmuir−Blodgett film deposition, shear stiffening by surface area cycling resulted in very compact films on transfer to a substrate.

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A Matter of Charge: Electrostatically Tuned Coassembly of Amphiphilic Peptides

Arad,

Levi,

Yosefi

et al. 2024

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Coassembly of peptide biomaterials offers a compelling avenue to broaden the spectrum of hierarchically ordered supramolecular nanoscale structures that may be relevant for biomedical and biotechnological applications. In this work coassemblies of amphiphilic and oppositely charged, anionic and cationic, β‐sheet peptides are studied, which may give rise to a diverse range of coassembled forms. Mixtures of the peptides show significantly lower critical coassembly concentration (CCC) values compared to those of the individual pure peptides. Intriguingly, the highest formation of coassembled fibrils is found to require excess of the cationic peptide whereas equimolar mixtures of the peptides exhibited the maximum folding into β‐sheet structures. Mixtures of the peptides coassembled sequentially from solutions at concentrations surpassing each peptide's intrinsic critical assembly concentration (CAC), are also found to require a higher portion of the cationic peptide to stabilize hydrogels. This study illuminates a systematic investigation of oppositely charged β‐sheet peptides over a range of concentrations, in solutions and in hydrogels. The results may be relevant to the fundamental understanding of such intricate charge‐driven assembly systems and to the formulation of peptide‐based nanostructures with diverse functionalities.

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Functional Peptide Monolayers at Interfaces

Cited by 4 publications

References 60 publications

Peptide self-assembly: thermodynamics and kinetics

Peptide self-assembly: thermodynamics and kinetics

Aligned Assembly in a 2-D Gel of a Water-Soluble Peptide

A Matter of Charge: Electrostatically Tuned Coassembly of Amphiphilic Peptides

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