Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

Klass, Sarah H.; Smith, MatthewJ.; Fiala, Tahoe A.; Lee, Jessica; Omole, Anthony; Downing, Kenneth H.; Francis, Matthew B.

doi:10.26434/chemrxiv.7157507.v1

Cited by 8 publications

(11 citation statements)

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“…A CMC of 5 µM is in the typical micro-molar range for peptide amphiphiles. 21,[42][43][44] The peptide's degree of disorder was experimentally verified by measuring the circular dichroism (CD) spectrum of samples of the peptide (unconjugated) and the two IDPA1 variants (Supplementary Figure S2). In addition, the peptide sequence displays a high probability for disorder and the absence of regular secondary structure using the NetSurfP-2.0 bioinformatic algorithm (Supplementary Figure S3).…”

Section: Resultsmentioning

confidence: 99%

Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

Jacoby¹,

Segal²,

Ehm³

et al. 2021

Preprint

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Amphiphilic molecules and their self-assembled structures have long been the target of extensive research due to their potential applications in fields ranging from materials design to biomedical and cosmetic applications. Increasing demands for functional complexity have been met with challenges in biochemical engineering, driving researchers to innovate in the design of new amphiphiles. An emerging class of molecules, namely, peptide amphiphiles, combines key advantages and circumvents some of the disadvantages of conventional phospholipids and block-copolymers. Herein, we present new peptide amphiphiles comprised of an intrinsically disordered peptide conjugated to two variants of hydrophobic dendritic domains. These molecules termed intrinsically disordered peptide amphiphiles (IDPA), exhibit a sharp pH-induced micellar phase-transition from low-dispersity spheres to extremely elongated worm-like micelles. We present an experimental characterization of the transition and propose a theoretical model to describe the pH-response. We also present the potential of the shape transition to serve as a mechanism for the design of a cargo hold-and-release application. Such amphiphilic systems demonstrate the power of tailoring the interactions between disordered peptides for various stimuli-responsive biomedical applications.

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Section: Resultsmentioning

confidence: 99%

Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

Jacoby¹,

Segal²,

Ehm³

et al. 2021

Preprint

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“…However, before polypeptide synthesis, a time-consuming process of genetic construction, optimisation, and troubleshooting is required. Furthermore, toxicity of the produced peptide to the host can lead to low or even zero yields, particularly in peptides that are short or tend to self-assemble [27]. The purification and extraction of the target peptides from the host cells can also be laborious and expensive requiring complex chromatographic techniques.…”

Section: Synthesis Of Polypeptidesmentioning

confidence: 99%

“…Polypeptides with more complex amino acid sequences can yield more controlled selfassembly behaviour than 'simpler' diblock copolypeptides [27,90,107]. ELPs, initially described by Urry and co-workers [108,109], are based on the pentamer sequence VPGXG, where X represents a guest residue and can be any amino acid except proline.…”

Section: The Hydrophobic Effect In Peptide Self-assemblymentioning

confidence: 99%

Designing peptide nanoparticles for efficient brain delivery

Duro‐Castaño

Leite

Forth

et al. 2020

Advanced Drug Delivery Reviews

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…After the synthesis, the globular soluble domain was removed to make selfassembling proteins containing a hydrophilic domain derived from intrinsically disordered proteins (IDPs) and a hydrophobic domain containing oligomers of hydrophobic tetrapeptides. 11 Although they were successful in making self-assembling proteins with moderate hydrophobicity, proteins with a high hydropathy index failed to express for the same reasons mentioned above. Similarly, Chilkoti and coworkers exploited the genetic method along with a post-translational modification strategy to make self-assembling lipidated proteins.…”

Section: ■ Introductionmentioning

confidence: 99%

Rapid Chemical Synthesis of Self-Assembling Semi-Synthetic Proteins

et al. 2021

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The design of well-defined monodispersed selfassembling semi-synthetic proteins is emerging as a promising research avenue. These proteins hold great potential to be used as scaffolds for various protein nanotechnology applications. Currently, there are very few chemical methods reported; however, they suffer from elaborate multistep organic synthesis. Herein, we report a new chemical methodology for the rapid synthesis of a diverse set of semi-synthetic protein families, which include protein amphiphiles, facially amphiphilic protein−dendron conjugates, and pH-sensitive protein−dendron conjugates. This chemical method holds great potential to access a wide variety of semi-synthetic proteins in a short time.

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Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

Cited by 8 publications

References 0 publications

Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

Designing peptide nanoparticles for efficient brain delivery

Rapid Chemical Synthesis of Self-Assembling Semi-Synthetic Proteins

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