Tuning Peptide Structure and Function through Fluorobenzene Stapling

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Standard

Tuning Peptide Structure and Function through Fluorobenzene Stapling. / Fischer, Niklas H.; Fumi, Erik; Oliveira, Maria Teresa; Thulstrup, Peter W.; Diness, Frederik.

I: Chemistry: A European Journal, Bind 28, Nr. 8, e202103788, 2022.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Fischer, NH, Fumi, E, Oliveira, MT, Thulstrup, PW & Diness, F 2022, 'Tuning Peptide Structure and Function through Fluorobenzene Stapling', Chemistry: A European Journal, bind 28, nr. 8, e202103788. https://doi.org/10.1002/chem.202103788

APA

Fischer, N. H., Fumi, E., Oliveira, M. T., Thulstrup, P. W., & Diness, F. (2022). Tuning Peptide Structure and Function through Fluorobenzene Stapling. Chemistry: A European Journal, 28(8), [e202103788]. https://doi.org/10.1002/chem.202103788

Vancouver

Fischer NH, Fumi E, Oliveira MT, Thulstrup PW, Diness F. Tuning Peptide Structure and Function through Fluorobenzene Stapling. Chemistry: A European Journal. 2022;28(8). e202103788. https://doi.org/10.1002/chem.202103788

Author

Fischer, Niklas H. ; Fumi, Erik ; Oliveira, Maria Teresa ; Thulstrup, Peter W. ; Diness, Frederik. / Tuning Peptide Structure and Function through Fluorobenzene Stapling. I: Chemistry: A European Journal. 2022 ; Bind 28, Nr. 8.

Bibtex

@article{c54b8e94763247d68e8e4459181877dc,
title = "Tuning Peptide Structure and Function through Fluorobenzene Stapling",
abstract = "Cyclic peptides are promising next-generation therapeutics with improved biological stability and activity. A catalyst-free stapling method for cysteine-containing peptides has been developed that enables fine-tuning of the macrocycle by using the appropriate regioisomers of fluorobenzene linkers. Stapling was performed on the unprotected linear peptide or, more conveniently, directly on-resin after peptide synthesis. NMR spectroscopy and circular dichroism studies demonstrate that the type of stapling can tune the secondary structures of the peptides. The method was applied to a set of potential agonists for melanocortin receptors, generating a library of macrocyclic potent ligands with ortho, meta or para relationships between the thioethers. Their small but significant differences in potency and efficacy demonstrate how the method allows facile fine-tuning of macrocyclic peptides towards biological targets from the same linear precursor.",
author = "Fischer, {Niklas H.} and Erik Fumi and Oliveira, {Maria Teresa} and Thulstrup, {Peter W.} and Frederik Diness",
year = "2022",
doi = "10.1002/chem.202103788",
language = "English",
volume = "28",
journal = "Chemistry: A European Journal",
issn = "0947-6539",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "8",

}

RIS

TY - JOUR

T1 - Tuning Peptide Structure and Function through Fluorobenzene Stapling

AU - Fischer, Niklas H.

AU - Fumi, Erik

AU - Oliveira, Maria Teresa

AU - Thulstrup, Peter W.

AU - Diness, Frederik

PY - 2022

Y1 - 2022

N2 - Cyclic peptides are promising next-generation therapeutics with improved biological stability and activity. A catalyst-free stapling method for cysteine-containing peptides has been developed that enables fine-tuning of the macrocycle by using the appropriate regioisomers of fluorobenzene linkers. Stapling was performed on the unprotected linear peptide or, more conveniently, directly on-resin after peptide synthesis. NMR spectroscopy and circular dichroism studies demonstrate that the type of stapling can tune the secondary structures of the peptides. The method was applied to a set of potential agonists for melanocortin receptors, generating a library of macrocyclic potent ligands with ortho, meta or para relationships between the thioethers. Their small but significant differences in potency and efficacy demonstrate how the method allows facile fine-tuning of macrocyclic peptides towards biological targets from the same linear precursor.

AB - Cyclic peptides are promising next-generation therapeutics with improved biological stability and activity. A catalyst-free stapling method for cysteine-containing peptides has been developed that enables fine-tuning of the macrocycle by using the appropriate regioisomers of fluorobenzene linkers. Stapling was performed on the unprotected linear peptide or, more conveniently, directly on-resin after peptide synthesis. NMR spectroscopy and circular dichroism studies demonstrate that the type of stapling can tune the secondary structures of the peptides. The method was applied to a set of potential agonists for melanocortin receptors, generating a library of macrocyclic potent ligands with ortho, meta or para relationships between the thioethers. Their small but significant differences in potency and efficacy demonstrate how the method allows facile fine-tuning of macrocyclic peptides towards biological targets from the same linear precursor.

U2 - 10.1002/chem.202103788

DO - 10.1002/chem.202103788

M3 - Journal article

C2 - 34897848

VL - 28

JO - Chemistry: A European Journal

JF - Chemistry: A European Journal

SN - 0947-6539

IS - 8

M1 - e202103788

ER -

ID: 290108167