Controlled self-assembly of α-helix-decorated peptide nanostructures

Choi, Sung Ju; Jeong, Woo Jin; Kim, Tae Hyun; Lim, Yong Beom

doi:10.1039/c0sm01275k

Cited by 17 publications

(22 citation statements)

References 33 publications

(33 reference statements)

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“…It is well known that α ‐helical structures play an important role in determining protein structures and functions []. Peptides with α ‐helical secondary structure are important building blocks in the field of molecular self‐assembly []. Some nanostructures are made by using peptides with α ‐helical conformation.…”

Section: Introductionmentioning

confidence: 99%

Nanostructures from the self-assembly of α -helical peptide amphiphiles

Meng¹,

Kou²,

Ma³

et al. 2014

J. Pept. Sci.

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Self-assembly of PAs composed of palmitic acid and several repeated heptad peptide sequences, C₁₅H₃₁CO-(IEEYTKK)(n)-NH₂ (n = 1-4, represented by PA1-PA4), was investigated systematically. The secondary structures of the PAs were characterized by CD. PA3 and PA4 (n = 3 and 4, respectively) showed an α-helical structure, whereas PA1 and PA2 (n = 1 and 2, respectively) did not display an α-helical conformations under the tested conditions. The morphology of the self-assembled peptides in aqueous medium was studied by transmission electron microscopy. As the number of heptad repeats in the PAs increased, the nanostructure of the self-assembled peptides changed from nanofibers to nanovesicles. Changes of the secondary structures and the self-assembly morphologies of PA3 and PA4 in aqueous medium with various cations were also studied. The critical micelle concentrations were determined using a pyrene fluorescence probe. In conclusion, this method may be used to design new peptide nanomaterials.

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Section: Introductionmentioning

confidence: 99%

Nanostructures from the self-assembly of α -helical peptide amphiphiles

Meng¹,

Kou²,

Ma³

et al. 2014

J. Pept. Sci.

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“…[54][55][56][57][58][59] To this aim, different stimuli have been used like polarity of the medium, pH, enzymatic reactions, dilution or the presence of chemicals and reducing agents. [60][61][62][63][64][65][66][67][68][69] Here we report on the design, synthesis and characterization of different Gemini Amphiphilic Pseudopeptides (thereafter named GAPs) 70 able to self-assemble into nanostructures displaying different shapes like fibers, tubes, tapes or vesicles. More interestingly, the self-assembling process can be controlled through the polarity of the environment and, for some specific examples, can be switched between fibers and vesicles by simple variation of the pH.…”

Section: Introductionmentioning

confidence: 99%

Stimulus responsive self-assembly of Gemini Amphiphilic Pseudopeptides

et al. 2011

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Registro de acceso restringido Este recurso no está disponible en acceso abierto por política de la editorial. No obstante, se puede acceder al texto completo desde la Universitat Jaume I o si el usuario cuenta con suscripción. Registre d'accés restringit Aquest recurs no està disponible en accés obert per política de l'editorial. No obstant això, es pot accedir al text complet des de la Universitat Jaume I o si l'usuari compta amb subscripció. Restricted access item This item isn't open access because of publisher's policy. The full--text version is only available from Jaume I University or if the user has a running suscription to the publisher's contents.

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“…The gradual decrease in the intensity of negative bands at t = 12 hours was observed for all the peptides suggesting the molecular aggregation due to intermolecular interactions. It has been reported that intermolecular interactions involved in peptides are important for self‐assembling and peptide nanostructures …”

Section: Resultsmentioning

confidence: 99%

“…It has been reported that intermolecular interactions involved in peptides are important for self-assembling and peptide nanostructures. [40][41][42] The self-assembled structures formed by the hybrid peptides P1…”

Section: Self-assembling Studiesmentioning

confidence: 99%

Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

Shankar

Singh

Rahim

et al. 2020

Journal of Peptide Science

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The present work describes the synthesis and characterization of α/γ hybrid peptides, Boc‐Phe‐γ4‐Phe‐Val‐OMe, P1; Boc‐Ala‐γ4‐Phe‐Val‐OMe, P2; and Boc‐Leu‐γ4‐Phe‐Val‐OMe, P3 together with the formation of self‐assembled structures formed by these hybrid peptides in dimethyl sulfoxide (DMSO)/water (1:1). The self‐assembled structures were characterized by infrared (IR) spectroscopy, circular dichroism (CD), and scanning electron microscopy (SEM). Further, α/γ hybrid peptide self‐assembled structures were evaluated for antibacterial properties. Among all, the self‐assembled peptide P1 exhibited the antimicrobial activity against Escherichia coli and Klebsiella pneumoniae, while self‐assembled peptide P3 inhibited the biofilms of Salmonella typhimurium and Pseudomonas aeruginosa. In this study, we have shown the significance of self‐assembled structures formed from completely hydrophobic α/γ hybrid peptides in exploring the antibacterial properties together with biofilm inhibition.

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Controlled self-assembly of α-helix-decorated peptide nanostructures

Abstract: This study describes a strategy to control the degree of a-helix stabilization and the shape of a-helix-decorated nanostructures. Coassembly of a macrocyclic peptide and a b-sheet peptide diminished steric clashes between helical peptide segments, further stabilizing a-helices.

Cited by 17 publications

References 33 publications

Nanostructures from the self-assembly of α -helical peptide amphiphiles

Nanostructures from the self-assembly of α -helical peptide amphiphiles

Stimulus responsive self-assembly of Gemini Amphiphilic Pseudopeptides

Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties

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