Aromatic–Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels

Li, Jie; Du, Xuewen; Hashim, Saqib; Shy, Adrianna N; Xu, Bing

doi:10.1021/jacs.6b11512

Cited by 136 publications

(107 citation statements)

References 49 publications

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“…In the past few decades,peptide hydrogels,i ns ome sense mimicking cytoskeleton and extracellular matrix, have attracted extensive interest due to their advantages of structural programmability,g ood biocompatibility and biodegradability as well as versatile functionality. [11] One typical building block for this case is the amyloid-derived diphenylalanine peptide modified with N-fluorenylmethoxycarbonyl (Fmoc-FF), which has been recently reported to form ordered nanofibrous structures. [9] They are able to self-assemble into well-ordered structures through amultiscale hierarchical assembly process driven by various intermolecular interactions including hydrophobic interaction, hydrogen bonding, p-p stacking, and van der Waals forces.…”

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confidence: 99%

Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix

et al. 2018

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Secondary structures such as α-helix and β-sheet are the major structural motifs within the three-dimensional geometry of proteins. Therefore, structure transitions from β-sheet to α-helix not only can serve as an effective strategy for the therapy of neurological diseases through the inhibition of β-sheet aggregation but also extend the application of α-helix fibrils in biomedicine. Herein, we present a charge-induced secondary structure transition of amyloid-derived dipeptide assemblies from β-sheet to α-helix. We unravel that the electrostatic (charge) repulsion between the C-terminal charges of the dipeptide molecules are responsible for the conversion of the secondary structure. This finding provides a new perspective to understanding the secondary structure formation and transformation in the supramolecular organization and life activity.

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confidence: 99%

Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix

et al. 2018

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“…There are few examples of the hydrogelation of α-helical peptides, which require more sophisticated design. [148] For example, Woolfson reported the first example of rationally designed and fully characterized self-assembling peptide hydrogels containing more than 99% water, based on linear peptides with purely α-helical structures. Two helices, formed by 28mers, wrapped around one another to form a dimer, with complete 3.5 residues per turn mediated by multiple hydrogen bonds.…”

Section: Supramolecular Hydrogels Made Of the Basic Biological Buimentioning

confidence: 99%

Supramolecular biofunctional materials

et al. 2017

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This review discusses supramolecular biofunctional materials, a novel class of biomaterials formed by small molecules that are held together via noncovalent interactions. The complexity of biology and relevant biomedical problems not only inspire, but also demand effective molecular design for functional materials. Supramolecular biofunctional materials offer (almost) unlimited possibilities and opportunities to address challenging biomedical problems. Rational molecular design of supramolecular biofunctional materials exploit powerful and versatile noncovalent interactions, which offer many advantages, such as responsiveness, reversibility, tunability, biomimicry, modularity, predictability, and, most importantly, adaptiveness. In this review, besides elaborating on the merits of supramolecular biofunctional materials (mainly in the form of hydrogels and/or nanoscale assemblies) resulting from noncovalent interactions, we also discuss the advantages of small peptides as a prevalent molecular platform to generate a wide range of supramolecular biofunctional materials for the applications in drug delivery, tissue engineering, immunology, cancer therapy, fluorescent imaging, and stem cell regulation. This review aims to provide a brief synopsis of recent achievements at the intersection of supramolecular chemistry and biomedical science in hope of contributing to the multidisciplinary research on supramolecular biofunctional materials for a wide range of applications. We envision that supramolecular biofunctional materials will contribute to the development of new therapies that will ultimately lead to a paradigm shift for developing next generation biomaterials for medicine.

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“…In each case,the compounds were heated and cooled to room temperature followed by ultra-sonication, [27] which produced self-supportable organogels.N ote that, ultra-sonication is not required for 9.D etailed gelation behavior of molecules 1-9 in toluene have been summarized in Table S1. [31] However,other heterochiral Fc-based peptides (2, 5, 7,and 8)produce solutions in toluene and are incapable of forming any kind of gel after prolonged ultra-sonication. Besides that, homochiral gels 1, 4,a nd 9 were stable and showed no change of state even after 24 h. Them etastable characteristic of heterochiral gels indicates that homochirality is an important factor for stable organogel formation.…”

Section: Determiningtheenigmaoftheoriginoflifeiscontroversialmentioning

confidence: 99%

On the Role of Chirality in Guiding the Self‐Assembly of Peptides

et al. 2017

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Homochirality in peptides is crucial in sustaining "like-like" intermolecular interactions that allow the formation of assemblies and aggregates and is ultimately responsible for the resulting material properties.Withthe help of aseries of stereoisomers of the tripeptide F-F-L, we demonstrate the critical role that peptide stereochemistry playsi nt he selfassembly of peptides,guided by molecular recognition, and for self-sorting.H omochiral self-assemblies are thermally and mechanically more robust compared to heterochiral selfassemblies.M orphological studies of the multicomponent peptide systems showed that aggregates formed from homochiral peptides possessed au niform nano-fibrous structure, whereas heterochiral systems resulted in self-sorted systems with ah eterogeneous morphology.I ne ssence,h omochiral peptides form the stronger aggregates,w hichm ay be one of reasons why homochirality is preferred in living systems.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

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Aromatic–Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels

Cited by 136 publications

References 49 publications

Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix

Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix

Supramolecular biofunctional materials

On the Role of Chirality in Guiding the Self‐Assembly of Peptides

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