Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4)

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4). / Mungalpara, Jignesh; Thiele, Stefanie; Eriksen, Øystein; Eksteen, Johann; Rosenkilde, Mette M; Våbenø, Jon.

In: Journal of Medicinal Chemistry, Vol. 55, No. 22, 09.10.2012, p. 10287-10291.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Mungalpara, J, Thiele, S, Eriksen, Ø, Eksteen, J, Rosenkilde, MM & Våbenø, J 2012, 'Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4)', Journal of Medicinal Chemistry, vol. 55, no. 22, pp. 10287-10291. https://doi.org/10.1021/jm300926y

APA

Mungalpara, J., Thiele, S., Eriksen, Ø., Eksteen, J., Rosenkilde, M. M., & Våbenø, J. (2012). Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4). Journal of Medicinal Chemistry, 55(22), 10287-10291. https://doi.org/10.1021/jm300926y

Vancouver

Mungalpara J, Thiele S, Eriksen Ø, Eksteen J, Rosenkilde MM, Våbenø J. Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4). Journal of Medicinal Chemistry. 2012 Oct 9;55(22):10287-10291. https://doi.org/10.1021/jm300926y

Author

Mungalpara, Jignesh ; Thiele, Stefanie ; Eriksen, Øystein ; Eksteen, Johann ; Rosenkilde, Mette M ; Våbenø, Jon. / Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4). In: Journal of Medicinal Chemistry. 2012 ; Vol. 55, No. 22. pp. 10287-10291.

Bibtex

@article{280834afd71b4dc8bc658d829e5e7eef,
title = "Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4)",
abstract = "In the absence of an experimentally determined binding mode for the cyclopentapeptide CXCR4 antagonists, we have rationally designed conformationally constrained analogues to further probe the small peptide binding pocket of CXCR4. Two different rigidification strategies were employed, both resulting in highly potent ligands (9 and 13). The information provided by this cyclopentapeptide ligand series will be very valuable in the development of novel peptidomimetic CXCR4 antagonists.",
keywords = "Drug Design, Humans, Ligands, Models, Molecular, Molecular Conformation, Peptides, Cyclic, Peptidomimetics, Protein Conformation, Receptors, CXCR4",
author = "Jignesh Mungalpara and Stefanie Thiele and {\O}ystein Eriksen and Johann Eksteen and Rosenkilde, {Mette M} and Jon V{\aa}ben{\o}",
year = "2012",
month = oct,
day = "9",
doi = "10.1021/jm300926y",
language = "English",
volume = "55",
pages = "10287--10291",
journal = "Journal of Medicinal Chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "22",

}

RIS

TY - JOUR

T1 - Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4)

AU - Mungalpara, Jignesh

AU - Thiele, Stefanie

AU - Eriksen, Øystein

AU - Eksteen, Johann

AU - Rosenkilde, Mette M

AU - Våbenø, Jon

PY - 2012/10/9

Y1 - 2012/10/9

N2 - In the absence of an experimentally determined binding mode for the cyclopentapeptide CXCR4 antagonists, we have rationally designed conformationally constrained analogues to further probe the small peptide binding pocket of CXCR4. Two different rigidification strategies were employed, both resulting in highly potent ligands (9 and 13). The information provided by this cyclopentapeptide ligand series will be very valuable in the development of novel peptidomimetic CXCR4 antagonists.

AB - In the absence of an experimentally determined binding mode for the cyclopentapeptide CXCR4 antagonists, we have rationally designed conformationally constrained analogues to further probe the small peptide binding pocket of CXCR4. Two different rigidification strategies were employed, both resulting in highly potent ligands (9 and 13). The information provided by this cyclopentapeptide ligand series will be very valuable in the development of novel peptidomimetic CXCR4 antagonists.

KW - Drug Design

KW - Humans

KW - Ligands

KW - Models, Molecular

KW - Molecular Conformation

KW - Peptides, Cyclic

KW - Peptidomimetics

KW - Protein Conformation

KW - Receptors, CXCR4

U2 - 10.1021/jm300926y

DO - 10.1021/jm300926y

M3 - Journal article

C2 - 23043442

VL - 55

SP - 10287

EP - 10291

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

SN - 0022-2623

IS - 22

ER -

ID: 138143015