Spontaneous construction of nanoperiodic architecture by two-dimensional self-assembly of an amphiphilic peptide–polyethylene glycol conjugate at the solid/water interface

Tanaka, Masayoshi; Abiko, Souhei; Koshikawa, Naokiyo; Katsuta, Masato; Kinoshita, Takatoshi

doi:10.1016/j.jcis.2013.11.054

Cited by 4 publications

(1 citation statement)

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“…104 Tanaka et al have reported that the conformation of AP in AP-PEG conjugates showed an interesting transition from randomcoils in aqueous solution to b-sheet structures at the solid/water interface. 105,106 The design and control of peptide self-assembly at the interface can be achieved by several factors. For instance, Gellman and Abbott et al found that the sequence of AP molecules is important for generating ordered monolayers on gold.…”

Section: The Kinetic Control Of Ap Self-assemblymentioning

confidence: 99%

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: 99%

Peptide self-assembly: thermodynamics and kinetics

et al. 2016

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Functional Peptide Monolayers at Interfaces

Leshem

Zarzhitsky

Rapaport

2015

Israel Journal of Chemistry

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Amphiphilic peptides can be designed to form ordered supramolecular structures at hydrophilic‐hydrophobic interfaces. These systems rely on the ability of peptides to fold into certain secondary structures at interfaces. This review focuses on the design of amphiphilic β‐sheet peptide assemblies in monolayers at interfaces, and their relevance to inducing mineralization and interactions with specific ions. In addition, the review discusses recent studies demonstrating the applicability of designed amphiphilic β‐sheet peptides to detection of specific small molecules and to elucidating intermolecular interactions relevant to drug delivery and enzyme catalysis systems.

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