Journal ArticleDOI
Amino acid sequence controls the self-assembled superstructure morphology of N-acetylated tri-β3-peptides
Rania S Seoudi,Annette Dowd,Mark P. Del Borgo,Ketav Kulkarni,Patrick Perlmutter,Mibel Aguilar,Adam Mechler +6 more
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TLDR
The effect of the topography of the 14-helical nanorod on lateral self-assembly is investigated and variations in the superstructure of three isomeric peptides comprising the same three β3-amino acid residues are reported on.Abstract:
Abstract Peptides based on unnatural β3-amino acids offer a versatile platform for the design of self-assembling nanostructures due to the folding stability of the 14-helix and the high symmetry of the side chains inherent in this geometry. We have previously described that N-terminal acetylation (Ac-) forms a supramolecular self-assembly motif that allows β3-peptides to assemble head-to-tail into a helical nanorod which then further bundles into hierarchical superstructures. Here we investigate the effect of the topography of the 14-helical nanorod on lateral self-assembly. Specifically, we report on the variations in the superstructure of three isomeric peptides comprising the same three β3-amino acid residues: β3-leucine (L), β3-isoleucine (I) β3-alanine (A) to give peptides Ac-β3[LIA], Ac-β3[IAL] and Ac-β3[ALI]. AFM imaging shows markedly different superstructures for the three peptides. Well defined synchrotron far-infrared spectra reveal uniform geometries with a high degree of similarity between the isomeric peptides in the amide modes of the 400–650 wavenumber range. Far-IR also confirms that the C-terminal carboxyl group is free in the assemblies, thus it is solvated in the dispersant. Hence, the differences in the superstructures formed by the fibers are defined primarily by van der Waals energy minimization between the varied cross sectional morphologies of the core nanorods.read more
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A self-assembling β-peptide hydrogel for neural tissue engineering
Sepideh Motamed,M.P. Del Borgo,Ketav Kulkarni,Nathan Habila,Kun Zhou,Patrick Perlmutter,John S. Forsythe,Marie-Isabel Aguilar +7 more
TL;DR: A new class of β-peptide based hydrogel for neural tissue engineering that shows excellent compatibility with neural cells and provides a suitable environment for cells to adhere and proliferate is reported.
Journal ArticleDOI
Geometrically Precise Building Blocks: the Self-Assembly of β-Peptides
TL;DR: The focus of this mini-review is on how the unique structural features of β-peptide assemblies have been exploited in the design of self-assembled proteomimetic bundles and nanomaterials.
Journal ArticleDOI
Hierarchical Nanomaterials Assembled from Peptoids and Other Sequence-Defined Synthetic Polymers.
Zhiliang Li,Zhiliang Li,Bin Cai,Bin Cai,Wenchao Yang,Wenchao Yang,Chun-Long Chen,Chun-Long Chen +7 more
TL;DR: A recent review as discussed by the authors summarizes the recent advances in the molecular self-assembly of hierarchical nanomaterials based on peptoids (or poly-N-substituted glycines) and other sequence-defined synthetic polymers.
Journal ArticleDOI
Novel Materials From the Supramolecular Self-Assembly of Short Helical β3-Peptide Foldamers.
TL;DR: This review provides an overview of self-assembled peptide nanostructures obtained via the supramolecular self-assembly of short β-peptide foldamers with a specific focus on N-acetyl-β3- peptides and their applications as bio- and nanomaterials.
Journal ArticleDOI
The Diverse World of Foldamers: Endless Possibilities of Self-Assembly.
TL;DR: In this review, selected articles will be analyzed to show the striking number of self-assemblies obtained for foldamers with different backbones, which will be analyze in order of increasing complexity.
References
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Journal ArticleDOI
Emerging biological materials through molecular self-assembly.
TL;DR: These self-assembling peptide systems represent a significant advance in the molecular engineering for diverse technological innovations and basic engineering principles for microfabrication can be learned by understanding the molecular self-assembly phenomena.
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Solution structure and dynamics of a de novo designed three-helix bundle protein.
TL;DR: The NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported, and it is now possible to design a complex protein with a well defined and predictable three-dimensional structure.
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Conformational analysis of linear peptides. 3. Temperature dependence of NH chemical shifts in chloroform
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Vibrational frequencies and modes of ?-helix
Koichi Itoh,Takehiko Shimanouchi +1 more
TL;DR: In this article, the normal vibration frequencies of the right-handed α-helix of poly-L-alanine and poly(L-α-amino-n-butyric acid) were calculated.
Journal ArticleDOI
Biomimetic Peptide Nanosensors
TL;DR: A novel platform for the development of highly sensitive and selective "nanoelectronic noses" based on natural peptide sequences or sequences identified from phage display as capture elements and molecular modeling provides detailed insights into the hybrid nanostructure.