Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)

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

Standard

Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). / Baumann, Markus; Hussain, Mohammad Musarraf; Henne, Nina; Garrote, Daniel Moya; Karlshoj, Stefanie; Fossen, Torgils; Rosenkilde, Mette M.; Vabeno, Jon; Haug, Bengt Erik.

In: Bioorganic & Medicinal Chemistry, Vol. 25, No. 2, 15.01.2017, p. 646-657.

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

Harvard

Baumann, M, Hussain, MM, Henne, N, Garrote, DM, Karlshoj, S, Fossen, T, Rosenkilde, MM, Vabeno, J & Haug, BE 2017, 'Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)', Bioorganic & Medicinal Chemistry, vol. 25, no. 2, pp. 646-657. https://doi.org/10.1016/j.bmc.2016.11.036

APA

Baumann, M., Hussain, M. M., Henne, N., Garrote, D. M., Karlshoj, S., Fossen, T., Rosenkilde, M. M., Vabeno, J., & Haug, B. E. (2017). Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). Bioorganic & Medicinal Chemistry, 25(2), 646-657. https://doi.org/10.1016/j.bmc.2016.11.036

Vancouver

Baumann M, Hussain MM, Henne N, Garrote DM, Karlshoj S, Fossen T et al. Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). Bioorganic & Medicinal Chemistry. 2017 Jan 15;25(2):646-657. https://doi.org/10.1016/j.bmc.2016.11.036

Author

Baumann, Markus ; Hussain, Mohammad Musarraf ; Henne, Nina ; Garrote, Daniel Moya ; Karlshoj, Stefanie ; Fossen, Torgils ; Rosenkilde, Mette M. ; Vabeno, Jon ; Haug, Bengt Erik. / Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). In: Bioorganic & Medicinal Chemistry. 2017 ; Vol. 25, No. 2. pp. 646-657.

Bibtex

@article{8ee936c498fc42b3b859858ec7cd4171,
title = "Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)",
abstract = "Here we report a series of close analogues of our recently published scaffold-based tripeptidomimetic CXCR4 antagonists, containing positively charged guanidino groups in R1 and R2, and an aromatic group in R3. While contraction/elongation of the guanidine carrying side chains (R1 and R2) resulted in loss of activity, introduction of bromine in position 1 on the naphth-2-ylmethyl moiety (R3) resulted in an EC50 of 61 μM (mixture of diastereoisomers) against wild-type CXCR4; thus, the antagonistic activity of these tripeptidomimetics seems to be amenable to optimization of the aromatic moiety. Moreover, for analogues carrying a naphth-2-ylmethyl substituent, we observed that a Pictet-Spengler like cyclization side reaction depended on the nature of the R1 substituent.",
keywords = "CXCR4 antagonist, Peptidomimetic, Scaffold",
author = "Markus Baumann and Hussain, {Mohammad Musarraf} and Nina Henne and Garrote, {Daniel Moya} and Stefanie Karlshoj and Torgils Fossen and Rosenkilde, {Mette M.} and Jon Vabeno and Haug, {Bengt Erik}",
year = "2017",
month = jan,
day = "15",
doi = "10.1016/j.bmc.2016.11.036",
language = "English",
volume = "25",
pages = "646--657",
journal = "Bioorganic & Medicinal Chemistry",
issn = "0968-0896",
publisher = "Pergamon Press",
number = "2",

}

RIS

TY - JOUR

T1 - Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)

AU - Baumann, Markus

AU - Hussain, Mohammad Musarraf

AU - Henne, Nina

AU - Garrote, Daniel Moya

AU - Karlshoj, Stefanie

AU - Fossen, Torgils

AU - Rosenkilde, Mette M.

AU - Vabeno, Jon

AU - Haug, Bengt Erik

PY - 2017/1/15

Y1 - 2017/1/15

N2 - Here we report a series of close analogues of our recently published scaffold-based tripeptidomimetic CXCR4 antagonists, containing positively charged guanidino groups in R1 and R2, and an aromatic group in R3. While contraction/elongation of the guanidine carrying side chains (R1 and R2) resulted in loss of activity, introduction of bromine in position 1 on the naphth-2-ylmethyl moiety (R3) resulted in an EC50 of 61 μM (mixture of diastereoisomers) against wild-type CXCR4; thus, the antagonistic activity of these tripeptidomimetics seems to be amenable to optimization of the aromatic moiety. Moreover, for analogues carrying a naphth-2-ylmethyl substituent, we observed that a Pictet-Spengler like cyclization side reaction depended on the nature of the R1 substituent.

AB - Here we report a series of close analogues of our recently published scaffold-based tripeptidomimetic CXCR4 antagonists, containing positively charged guanidino groups in R1 and R2, and an aromatic group in R3. While contraction/elongation of the guanidine carrying side chains (R1 and R2) resulted in loss of activity, introduction of bromine in position 1 on the naphth-2-ylmethyl moiety (R3) resulted in an EC50 of 61 μM (mixture of diastereoisomers) against wild-type CXCR4; thus, the antagonistic activity of these tripeptidomimetics seems to be amenable to optimization of the aromatic moiety. Moreover, for analogues carrying a naphth-2-ylmethyl substituent, we observed that a Pictet-Spengler like cyclization side reaction depended on the nature of the R1 substituent.

KW - CXCR4 antagonist

KW - Peptidomimetic

KW - Scaffold

U2 - 10.1016/j.bmc.2016.11.036

DO - 10.1016/j.bmc.2016.11.036

M3 - Journal article

C2 - 27939345

VL - 25

SP - 646

EP - 657

JO - Bioorganic & Medicinal Chemistry

JF - Bioorganic & Medicinal Chemistry

SN - 0968-0896

IS - 2

ER -

ID: 173778105