Conformational stability studies of a stapled hexa-β3-peptide library

Gopalan, Romila D.; Borgo, Mark P. Del; Bergman, Ylva Elisabet; Unabia, Sharon; Mulder, Roger J.; Wilce, Matthew C. J.; Wilce, Jacqueline Anne; Aguilar, Marie‐Isabel; Perlmutter, Patrick

doi:10.1039/c2ob06617c

Cited by 14 publications

(7 citation statements)

References 16 publications

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“…presence of secondary structure which in the case of β 3 -peptides is consistent with a 14-helix (Bergman et al, 2009;Gopalan et al, 2012).…”

Section: Lipidation Of Tri-β 3 -Peptide Monomers Leads To Fibers Of Umentioning

confidence: 57%

“…The side chains can be positioned at either the α-or β-carbon, resulting in either β 2 or β 3 -amino acids. β 3 -Peptides have been shown to adopt well-defined helical structures stabilized by hydrogen bonding interactions (Appella et al, 1997;Seebach et al, 2006;Gopalan et al, 2012). Peptides comprised solely of acyclic β 3 -amino acids predominantly adopt a 14-helical conformation (Raguse et al, 2001;Seebach et al, 2006;Bergman et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers

et al. 2020

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β 3-peptides consisting exclusively of β 3-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphology, a lipid moiety was introduced within a tri-β 3-peptide sequence at each of the three amino acid positions and the N-terminus to gain finer control over the lateral assembly of fibers. Depending on the position of the lipid, the self-assembled structures formed either twisted ribbon-like fibers or distinctive multilaminar nanobelts. The nanobelt structures were comprised of multiple layers of peptide fibrils as revealed by puncturing the surface of the nanobelts with an AFM probe. This stacking phenomenon was completely inhibited through changes in pH, indicating that the layer stacking was mediated by electrostatic interactions. Thus, the present study is the first to show controlled self-assembly of these fibrous structures, which is governed by the location of the acyl chain in combination with the 3-point H-bonding motif. Overall, the results demonstrate that the nanostructures formed by the β 3-tripeptide foldamers can be tuned via sequential lipidation of N-acetyl β 3-tripeptides which control the lateral interactions between peptide fibrils and provide defined structures with a greater homogeneous population.

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“…presence of secondary structure which in the case of β 3 -peptides is consistent with a 14-helix (Bergman et al, 2009;Gopalan et al, 2012).…”

Section: Lipidation Of Tri-β 3 -Peptide Monomers Leads To Fibers Of Umentioning

confidence: 57%

Section: Introductionmentioning

confidence: 99%

Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers

et al. 2020

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“…The relative thickness of the fibers suggests higher order hierarchical self‐assembly. While the substructure of the large fibers could not be resolved by light microscopy, hexa‐β 3 ‐peptides 3 and 4 22 and tri‐β 3 ‐peptides 5 and 6 formed thinner fibers which proved more amenable. Images of these fibers clearly show a twisted ribbonlike morphology (Figure 3).…”

Section: β3‐peptides Used In This Study (N‐acetyl Caps Highlighted Inmentioning

confidence: 96%

Supramolecular Self‐Assembly of N‐Acetyl‐Capped β‐Peptides Leads to Nano‐ to Macroscale Fiber Formation

et al. 2013

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From little things big things grow: 14‐Helical N‐acetyl β3‐peptides spontaneously self‐assemble in a unique head‐to‐tail fashion to form fibers from solution. The fiber size can be controlled from the nano‐ to the macroscale. The inherent flexibility in design and ease of synthesis provide powerful new avenues for the development of novel bio‐ and nanomaterials by supramolecular self‐assembly.

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“…The relative thickness of the fibers suggests higher order hierarchical self-assembly. While the substructure of the large fibers could not be resolved by light microscopy, hexa-b 3peptides 3 and 4 [22] and tri-b 3 -peptides 5 and 6 formed thinner fibers which proved more amenable. Images of these fibers clearly show a twisted ribbonlike morphology (Figure 3).…”

mentioning

confidence: 93%

“…While the substructure of the large fibers could not be resolved by light microscopy, hexa-b 3 peptides 3 and 4 [22] and tri-b 3 -peptides 5 and 6 formed thinner fibers which proved more amenable. Images of these fibers clearly show a twisted ribbonlike morphology (Figure 3 The presence of the different-sized fibers with helical periodicity suggests a mechanism of hierarchical self-assembly that follows a multistep "self-twining" process by means of the formation of consecutively higher order ropelike nanofibers from individual fibrils (Figure 4 B and see also Figure 6 G-I).…”

mentioning

confidence: 97%

Supramolecular Self‐Assembly of N‐Acetyl‐Capped β‐Peptides Leads to Nano‐ to Macroscale Fiber Formation

et al. 2013

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Aus kleinen Dingen werden große: 14‐Helicale N‐Acetyl‐β3‐peptide bilden in Lösung spontan in einer einzigartigen Kopf‐Schwanz‐Verknüpfung Fasern. Die Fasergröße lässt sich vom Nano‐ bis zum Makrobereich einstellen. Die inhärente Flexibilität im Design und die einfache Synthese bieten neue leistungsfähige Möglichkeiten für die Entwicklung von Bio‐ und Nanomaterialien durch supramolekulare Selbstorganisation.

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Conformational stability studies of a stapled hexa-β3-peptide library

Cited by 14 publications

References 16 publications

Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers

Transition of Nano-Architectures Through Self-Assembly of Lipidated β3-Tripeptide Foldamers

Supramolecular Self‐Assembly of N‐Acetyl‐Capped β‐Peptides Leads to Nano‐ to Macroscale Fiber Formation

Supramolecular Self‐Assembly of N‐Acetyl‐Capped β‐Peptides Leads to Nano‐ to Macroscale Fiber Formation

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