Macroscale assembly of peptide nanotubes

Lu, Kun Ping; Guo, Liang; Mehta, Anil K.; Childers, W. Seth; Dublin, Steven N.; Skanthakumar, S.; Conticello, Vincent P.; Thiyagarajan, P.; Apkarian, Robert P.; Lynn, David G.

doi:10.1039/b701029j

Cited by 62 publications

(85 citation statements)

References 10 publications

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“…The precisely patterned surfaces of the Aβ(16-22) nanotubes are composed of positively charged lysine (blue) knobs and leucine-rich hydrophobic groves (gray) as shown in Fig 4B [57]. An interesting outcome of this patterning is seen at CR saturation, which sufficiently passivates the surface and bundles the hollow nanotubes in a manner similar to sulfate [60] into higher order millimeter long supramacromolecular fibers similar to those shown in Fig. 1B.…”

Section: Introductionmentioning

confidence: 99%

Peptide membranes in chemical evolution☆

Childers

Mehta

et al. 2009

Current Opinion in Chemical Biology

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SUMMARYSimple surfactants achieve remarkable long-range order in aqueous environments. This organizing potential is seen most dramatically in biological membranes where phospholipid assemblies both define cell boundaries and provide a ubiquitous structural scaffold for controlling cellular chemistry. Here we consider simple peptides that also spontaneously assemble into exceptionally ordered scaffolds, and review early data suggesting that these structures maintain the functional diversity of proteins. We argue that such scaffolds can achieve the required molecular order and catalytic agility for the emergence of chemical evolution.

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Section: Introductionmentioning

confidence: 99%

Peptide membranes in chemical evolution☆

Childers

Mehta

et al. 2009

Current Opinion in Chemical Biology

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“…Both SAP and PA nanofibers can further assemble into macrostructures that resemble components of native extracellular tissue. 5,6 Together, these properties enable scaffold architectural design on both a nano and macro scale. For most SAPs, assembly has been engineered to occur at a physiologic pH, allowing solutions of these peptides to be injected into damaged tissues before assembling into hydrogels.…”

Section: Introductionmentioning

confidence: 99%

Self-assembling peptides for stem cell and tissue engineering

et al. 2016

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Regenerative medicine holds great potential to address many shortcomings in current medical therapies. An emerging avenue of regenerative medicine is the use of self-assembling peptides (SAP) in conjunction with stem cells to improve the repair of damaged tissues. The specific peptide sequence, mechanical properties, and nanotopographical cues vary widely between different SAPs, many of which have been used for the regeneration of similar tissues. To evaluate the potential of SAPs to guide stem cell fate, we extensively reviewed the literature for reports of SAPs and stem cell differentiation. To portray the most accurate summary of these studies, we deliberately discuss both the successes and pitfalls, allowing us to make conclusions that span the breadth of this exciting field. We also expand on these conclusions by relating these findings to the fields of nanotopography, mechanotransduction, and the native composition of the extracellular matrix in specific tissues to identify potential directions for future research.

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“…Although selfassembling β-sheet peptides based on amyloid and related de novo amino acid sequences are being actively scrutinized as functional nanoscale materials [3][4][5][6][7][8][9][10][11][12][13], the design of selfassembled fibrils derived from α-helical peptides [14,15] has not advanced to a similar extent. Helical scaffolds differ in critical structural features from β-sheet assemblies, including the structural periodicity of the fibre repeat [1], the orientation of protomers relative to the long axis of the fibril [16] and the physical interactions that guide self-association.…”

Section: Introductionmentioning

confidence: 99%

Engineering responsive mechanisms to control the assembly of peptide-based nanostructures

Dublin

Zimenkov

Conticello

2009

Biochemical Society Transactions

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Complex biological machines arise from self-assembly on the basis of structural features programmed into sequence-specific macromolecules (i.e. polypeptides and polynucleotides) at the molecular level. As a consequence of the near-absolute control of macromolecular architecture that results from such sequence specificity, biological structural platforms may have advantages for the creation of functional supramolecular assemblies in comparison with synthetic polymers. Thus biological structural motifs present an attractive target for the synthesis of artificial nanoscale systems on the basis of relationships between sequence and supramolecular structure that have been established for native biological assemblies. In the present review, we describe an approach to the creation of structurally defined supramolecular assemblies derived from synthetic alpha-helical coiled-coil structural motifs. Two distinct challenges are encountered in this approach to materials design: the ability to recode the canonical sequences of native coiled-coil structural motifs to accommodate the formation of structurally defined supramolecular assemblies (e.g. synthetic helical fibrils) and the development of methods to control supramolecular self-assembly of these peptide-based materials under defined conditions that would be amenable to conventional processing methods. In the present review, we focus on the development of mechanisms based on guest-host recognition to control fibril assembly/disassembly. This strategy utilizes the latent structural specificity encoded within sequence-defined peptides to couple a conformational transition within the coiled-coil motifs to incremental changes in environmental conditions. The example of a selective metal-ion-induced conformational switch will be employed to validate the design principles.

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Macroscale assembly of peptide nanotubes

Abstract: Simple oligopeptides that self-assemble into homogeneous nanotubes can be directed to further assemble into macroscale parallel arrays through protein "salting out" strategies.

Cited by 62 publications

References 10 publications

Peptide membranes in chemical evolution☆

Peptide membranes in chemical evolution☆

Self-assembling peptides for stem cell and tissue engineering

Engineering responsive mechanisms to control the assembly of peptide-based nanostructures

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