Hydrophobic-Region-Induced Transitions in Self-Assembled Peptide Nanostructures

Xu, Hai; Wang, Jing; Han, Song; Wang, Jiqian; Yu, Daoyong; Zhang, Hongyu; Xia, Daohong; Zhao, Xiubo; Waigh, Thomas A.; Lu, Jian R.

doi:10.1021/la802499n

Cited by 143 publications

(195 citation statements)

References 42 publications

(102 reference statements)

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“…As shown in Figure 1, the N-and C-termini of the peptides were acetylated and amidated, respectively, to eliminate the effect of terminal charges that are believed to complicate the process of selfassembly. The detailed procedures have been described in our previous work [30][31][32][33]. Deprotection, activation, coupling and capping were carried out on the synthesizer and cleavage from the resin was finished manually away from the synthesizer.…”

Section: Peptide Synthesismentioning

confidence: 99%

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Cao

Fan

et al. 2012

Chin. Sci. Bull.

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Hydrogels resulting from the self-assembly of small peptides are smart nanobiomaterials as their nanostructuring can be readily tuned by environmental stimuli such as pH, ionic strength and temperature, thereby favoring their practical applications. This work reports experimental observations of formation of peptide hydrogels in response to the redox environment. Ac-I 3 K-NH 2 is a short peptide amphiphile that readily self-assembles into long nanofibers and its gel formation occurs at concentrations of about 10 mmol/L. Introduction of a Cys residue into the hydrophilic region leads to a new molecule, Ac-I 3 CGK-NH 2 , that enables the formation of disulfide bonds between self-assembled nanofibers, thus favoring cross-linking and promoting hydrogel formation. Under oxidative environment, Ac-I 3 CGK-NH 2 formed hydrogels at much lower concentrations (even at 0.5 mmol/L). Furthermore, the strength of the hydrogels could be easily tuned by switching between oxidative and reductive conditions and time. However, AFM, TEM, and CD measurements revealed little morphological and structural changes at molecular and nano dimensions, showing no apparent influence arising from the disulfide bond formation.peptide amphiphiles, self-assembly, hydrogelation, redox stimuli Citation:Cao C H, Cao M W, Fan H M, et al. Redox modulated hydrogelation of a self-assembling short peptide amphiphile.

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Section: Peptide Synthesismentioning

confidence: 99%

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Cao

Fan

et al. 2012

Chin. Sci. Bull.

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“…However, for β-sheet forming SLPs, the self-assembled geometries do show some dependence on their hydrophobicity. In the case of Ac-A m K-NH 2 (m = 3, 6, 9), the three peptides all adopt predominantly β-sheet structures but form different morphologies: stacked bilayers (Ac-A 3 K-NH 2 ), long cylindrical nanofibrils (Ac-A 6 K-NH 2 ), and short nanorods and micelles (Ac-A 9 K-NH 2 ) ( Figure 3) [58]. Ac-I m K-NH 2 (m = 3, 4, 5) all form nanofibrils with predominantly β-sheet structures but their diameters decrease with an increase in the number of hydrophobic residues [54].…”

Section: Hydrophobic Interactionmentioning

confidence: 99%

“…The dimensional reduction can be interpreted using the molecular packing theory developed to describe surfactant structural transitions. With increasing hydrophobic tail length, the entropic gain, decreased CACs, and increased electrostatic repulsion between the head groups lead to a lowering of the packing parameter (p) [58]. It is widely accepted that spherical micelles form with 0  p  1/3, cylindrical micelles form with 1/3  p  1/2, and bilayer or lamellar sheets form with 1/2  p  1 [73].…”

Section: Hydrophobic Interactionmentioning

confidence: 99%

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Self-assembly of surfactant-like peptides and their applications

et al. 2014

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Numerous peptides derived from naturally occurring proteins or de novo designed have been found to self-assemble into various nanostructures. These well-defined nanostructures have shown great potential for a variety of biomedical and biotechnological applications. In particular, surfactant-like peptides (SLPs) have distinctive advantages in their length, aggregating ability, and water solubility. In this article, we report recent advances in the mechanistic understanding of the self-assembly principles of SLPs and in their applications, most of which have been made in our laboratory. Hydrogen bonding between peptide backbones, hydrophobic interaction between hydrophobic side chains, and electrostatic repulsion between charged head groups all have roles in mediating the self-assembly of SLPs; the final self-assembled nanostructures are therefore dependent on their interplay. SLPs have shown diverse applications ranging from membrane protein stabilization and antimicrobial/anticancer agents to nanofabrication and biomineralization. Future advances in the self-assembly of SLPs will hinge on their large-scale production, the design of new functional SLPs with targeted properties, and the exploitation of new or improved applications. surfactant-like peptides, self-assembly, mechanism, applications

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“…Over the years, the preference to study the behavioral growth of self-assembled peptide nanostructures (SPNs) has expanded [3,4] due to its biocompatibility and chemical diversity. Many short amphiphilic peptides are commonly used as scaffolds to produce inorganic materials that are in one-, two-or threedimensions at nano-scale [5,6].…”

Section: Introductionmentioning

confidence: 99%

Effect of Anions on Nanofiber Formation of β-sheet Propensity Amphiphile Peptide

Shamsudeen

Tan²,

Eshak³

2018

IOP Conf. Ser.: Mater. Sci. Eng.

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Force and time-dependent self-assembly, disruption and recovery of supramolecular peptide amphiphile nanofibers F Begum Dikecoglu, Ahmet E Topal, Alper D Ozkan et al.Self-assembly behaviors of molecular designer functional RADA16-I peptides: influence of motifs, pH, and assembly time Yuqiao Sun, Yongnu Zhang, Lingling Tian et al. Abstract. Peptide self-assembly forms different nanostructures under simple alteration in the solution environment. Understanding the mechanism of the assembly will help us to control and tailor functional nanomaterials. This study aims to investigate the influence of anions on the self-assembly morphology and shape using a synthetic peptide of FFFFKK. Circular Dichoism (CD) and Environmental Scanning Electron Microscope (ESEM) were used to determine the secondary structure and self-assembly morphology, while Image J imaging software was used to measure diameter size. In the absence of anion, FFFFKK formed antiparallel β-sheet that adopted sizeable fibrillar structure with a minimal increment over the first 7 hours of assembly. Irregular structure was observed in the presence of Iodide ion (I -) with a less stable secondary structure such as β-turn and β-loop. In the presence of perchlorate ion (ClO 4 -), needle-like structure was observed with predominantly β-sheet structure. Our study showed that peptide morphology can be controlled by using different anions with careful selection of amino acid residues in peptide sequence. IntroductionMolecular self-assembling is the association of molecular building blocks that spontaneously organized into ordered macroscopic structure by non-covalent bond without external control [1,2]. Over the years, the preference to study the behavioral growth of self-assembled peptide nanostructures (SPNs) has expanded [3,4] due to its biocompatibility and chemical diversity. Many short amphiphilic peptides are commonly used as scaffolds to produce inorganic materials that are in one-, two-or threedimensions at nano-scale [5,6]. These peptides have also been successfully used to fabricate materials with well-defined size and shape that have applications in various industry such as drug delivery, wound healing and tissue engineering [7][8][9]. The assembly mechanism occurs within the existence of several factors including peptide-peptide interaction [2]. However, interruption of external stimuli such as anions and changes in pH or temperature will cost the interaction of either forming a functional or non-functional structure [2]. These self-assembling structures are relatively discrete and unstable. Therefore, the ability to control the rational design peptides into targeted structures at the early stages of self-assembly should be further developed. This study provided insights into the role of anions on the structure formation over the first seven hours of the assembly. We designed a synthetic peptide, Ac-FFFFKK-CONH 2 that consist of four hydrophobic amino acids, phenylalanine, (F) and two positively charge hydrophilic amino acids, lysine, (K) at pH 7. The...

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Hydrophobic-Region-Induced Transitions in Self-Assembled Peptide Nanostructures

Cited by 143 publications

References 42 publications

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Redox modulated hydrogelation of a self-assembling short peptide amphiphile

Self-assembly of surfactant-like peptides and their applications

Effect of Anions on Nanofiber Formation of β-sheet Propensity Amphiphile Peptide

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