Bike peptides: a ride through the membrane

García-Pindado, Júlia; Royo, Soledad; Teixidó, Meritxell; Giralt, Ernest

doi:10.1002/psc.2993

Cited by 9 publications

(9 citation statements)

References 44 publications

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“…Earlier studies of our group demonstrated that the incorporation of an extra cyclization increases considerably the biostability in human serum. The published results demonstrated outstanding values of protease resistance, which can be quite beneficial.…”

Section: Resultsmentioning

confidence: 84%

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Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides

et al. 2018

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While revisiting biologically active natural peptides, the importance of the tryptophan residue became clear. In this article, the incorporation of this amino acid, brominated at different positions of the indole ring, into cyclic peptides was successfully achieved. These products demonstrated improved properties in terms of passive diffusion, permeability across membranes, biostability in human serum and cytotoxicity. Moreover, these brominated tryptophans at positions 5, 6, or 7 proved to be compatible as building blocks to prepare bicyclic stapled peptides by performing on-resin Suzuki-Miyaura cross-coupling reactions.

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Section: Resultsmentioning

confidence: 84%

“…The peptide was prepared using the standard methodology of García‐Pindado et al p NZ‐(7Br)Trp‐OH and Fmoc‐(7Br)Trp‐OH were used as the second and fourth amino acids, respectively. The synthesis was performed on solid‐phase using Fmoc/ t Bu chemistry.…”

Section: Methodsmentioning

confidence: 99%

Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides

et al. 2018

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“…The synthesis of bicyclic peptides containing a biaryl bridge and a cyclic backbone was described by García‐Pindado et al. in 2017, in which the cross‐coupling reaction took place between a boronophenylalanine and a iodophenylalanine to generate the biaryl bridge on resin . This approach was extended to bromotryptophan containing peptides in 2018 .…”

Section: Suzuki–miyaura Cross‐couplingmentioning

confidence: 99%

“…The serum stability of the bicyclic tryptophan peptides was not investigated . However, the previous study on a bicyclic peptide with a phenylalanine–phenylalanine biaryl bridge did not show any significant degradation in human serum within 24 h …”

Section: Suzuki–miyaura Cross‐couplingmentioning

confidence: 99%

Late‐Stage Diversification of Tryptophan‐Derived Biomolecules

Gruß

Sewald

2020

Chemistry A European J

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Pd-mediated reactions have emergeda sapowerful tool for the site-selective and bioorthogonall ate-stage diversification of amino acids, peptides and related compounds. Indole moieties of tryptophan derivatives are susceptible to C 2 H-activation, whereas halogenated aromatic amino acids such as halophenylalanines or halotryptophans provide ab road spectrum of different functionalisations. The compatibility of transition-metal-catalysed cross-couplings with functional groups in peptides, other biologically active compoundsa nd even proteins hasb een demonstrated. ThisReview primarily compiles the applicationo fd ifferent crosscoupling reactions to modify halotryptophans,h alotryptophan containing peptides or halogenated, biologically active compounds derived from tryptophan. Moderna pproaches use regio-and stereoselective biocatalytic strategies to generate halotryptophans and derivatives on ap reparative scale. The combination of bio-and chemocatalysis in cascade reactions is given by the biocompatibility and bioorthogonality of Pd-mediated reactions. Pd-Catalysed C 2 ÀHA ctivationo fT ryptophansThe C 2 position of indoles and tryptophans can be selectively addressed by transition-metal-catalysed C(sp 2 )ÀHa ctiva- [a] H. Gruß,P rof. Dr.N.S ewald

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“…The formation of the biaryl bond has been achieved via a Suzuki-Miyaura cross-coupling reaction, a Pd-catalyzed C-H activation or a Cu-mediated oxidative coupling. The former reaction has allowed the synthesis of peptides containing a Trp-Tyr [4,15], a Phe-Phe [15][16][17][18], a Phe-Tyr [15,17,19] or a Tyr-Tyr [15,[19][20][21] linkage. The C-H activation reaction has been used to form the biaryl bonds Trp-Phe and Trp-Tyr [22,23], while the Cumediated oxidative phenol coupling has provided access to peptides bearing a Tyr-hydroxyphenylglycine motif [24].…”

Section: Introductionmentioning

confidence: 99%

Solid-phase synthesis of biaryl cyclic peptides containing a histidine-tyrosine linkage

et al. 2019

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A solid-phase strategy for the synthesis of biaryl cyclic peptides containing a side-chain to sidechain His-Tyr linkage was developed. The key step was the macrocyclization of a linear peptidyl resin incorporating a 5-bromohistidine and a 3-boronotyrosine via the formation of the biaryl bond by means of a microwave-assisted Suzuki-Miyaura reaction. This method allowed direct access to biaryl cyclic peptides containing a 3-or 5-amino acid ring and bearing the histidine residue at the Nor the C-terminus, being especially conducive for analogues in which this amino acid is located at the C-terminus. This study also served to establish a strategy for the synthesis of biaryl cyclic peptides derived from the two hemispheres of the natural biaryl bicyclic peptides aciculitins.

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Bike peptides: a ride through the membrane

Cited by 9 publications

References 44 publications

Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides

Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides

Late‐Stage Diversification of Tryptophan‐Derived Biomolecules

Solid-phase synthesis of biaryl cyclic peptides containing a histidine-tyrosine linkage

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