Molecular Apple Peels

Garric, Joachim; Léger, Jean‐Michel; Huc, Ivan

doi:10.1002/anie.200462898

Cited by 149 publications

(52 citation statements)

References 54 publications

(11 reference statements)

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“…There are many examples of foldamers that are water soluble [62,[71][72][73][74], but in terms of hosts designed to bind guest molecules, they are relatively few. Indeed recent efforts in this area have focused on the reverse: that is, the encapsulation of polar molecules for solubilization in organic solvents or transport across bilayers [64,67,75,76]. An example of the creation of a hydrophobic pocket in a foldamer from the Moore group is the m-phenylene ethynylene 1.…”

Section: Common Classes Of Water-soluble Hostsmentioning

confidence: 99%

Van Der Waals Interactions and the Hydrophobic Effect

Gibb

2011

Chemosensors

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Section: Common Classes Of Water-soluble Hostsmentioning

confidence: 99%

Van Der Waals Interactions and the Hydrophobic Effect

Gibb

2011

Chemosensors

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“…Moreover, folding into conformationally stable structures, they could interact with various targets such as proteins, 2 membranes, 3 and so on. Up to now, oligomeric architectures including β -peptides, 4 peptoids, 5 β -peptoids, 6 oligoureas, 7 aza-peptides, 8 α -aminoisobutyric acid foldamers, 9 oligoproline, 10 aromatic amide foldamers, 11 and others have been well documented on the basis of either homogeneous or heterogeneous backbones, leading to various applications in molecular self-assembly and recognition. 12 Certain peptides consisting of both D-amino acids and L-amino acids were studied for their helicity; 13 however, it is very challenging to predict the folding propensity of the mixed peptides due to the intrinsic opposite folding propensity of D- and L-amino acids.…”

Section: Introductionmentioning

confidence: 99%

Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides

Teng

Cerrato

et al. 2017

J. Am. Chem. Soc.

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New types of foldamer scaffolds are formidably challenging to design and synthesize, yet highly desirable as structural mimics of peptides/proteins with a wide repertoire of functions. In particular, the development of peptidomimetic helical foldamers holds promise for new biomaterials, catalysts, and drug molecules. Unnatural L-sulfono-γ-AApeptides were recently developed and shown to have potential applications in both biomedical and material sciences. However, D-sulfono-γ-AApeptides, the enantiomers of L-sulfono-γ-AApeptides, have never been studied due to the lack of high-resolution three-dimensional structures to guide structure-based design. Herein, we report the first synthesis and X-ray crystal structures of a series of 2:1 L-amino acid/D-sulfono-γ-AApeptide hybrid foldamers, and elucidate their folded conformation at the atomic level. Single-crystal X-ray crystallography indicates that this class of oligomers folds into well-defined right-handed helices with unique helical parameters. The helical structures were consistent with data obtained from solution 2D NMR, CD studies, and molecular dynamics simulations. Our findings are expected to inspire the structure-based design of this type of unique folding biopolymers for biomaterials and biomedical applications.

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“…A broad range of folded structures have been constructed, including helices ( Figure 1), 27,28 novel folds 29 (e.g., herringbone helix 30 ), capsules, 31 and tertiary objects. 32 The synthesis of macrocyclic structures from folded oligomers 23,33,34 that function as receptors 23,[35][36][37][38][39][40] has stemmed from these endeavors.…”

Section: Scheme 1 Selected Conformational Preference Of Amide Bonds Imentioning

confidence: 99%

Synthesis of Oligobenzamide α-Helix Mimetics

Burslem

Wilson

2013

Synlett

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The development of inhibitors of protein-protein interactions (PPIs) represents a major challenge in chemical biology. α-Helix-mediated PPIs represent a subclass that might be amenable to inhibition using scaffolds that reproduce the spatial projection of recognition groups produced by the helix; these ligands are termed proteomimetics. Such a generic scaffold approach requires robust chemistry that can be used to synthesize reasonably large libraries of compounds. Foldamers are defined as oligomers that adopt welldefined folded structures. An ultimate goal of research in this area is to be able to reproduce and surpass the functionality of natural biopolymers; again a key enabling technology in this pursuit is robust synthetic methodology with a broad substrate scope. When we started our research program in this area seven years ago, we were drawn to aromatic oligoamide foldamers as potential proteomimetic scaffolds; however, in contrast to more widely studied β-peptideand peptoid-based foldamers, the synthesis of aromatic oligoamides was less well developed in terms of monomer diversity and amenability to library synthesis. This account describes our efforts and, more generally, the development of methodologies for the synthesis of aromatic oligoamides during this period.

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Molecular Apple Peels

Cited by 149 publications

References 54 publications

Van Der Waals Interactions and the Hydrophobic Effect

Van Der Waals Interactions and the Hydrophobic Effect

Right-Handed Helical Foldamers Consisting of De Novo d-AApeptides

Synthesis of Oligobenzamide α-Helix Mimetics

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