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dc.contributor.authorBaumann, Markus
dc.contributor.authorHussain, Mohammad Musarraf
dc.contributor.authorHenne, Nina
dc.contributor.authorGarrote, Daniel Moya
dc.contributor.authorKarlshøj, Stefanie
dc.contributor.authorFossen, Torgils
dc.contributor.authorRosenkilde, Mette M.
dc.contributor.authorVåbenø, Jon
dc.contributor.authorHaug, Bengt Erik
dc.PublishedBaumann M, Hussain MM, Henne N, Garrote DM, Karlshøj S, Fossen T, Rosenkilde MM, Våbenø J, Haug BE. Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). Bioorganic & Medicinal Chemistry. 2017;25(2):646-657eng
dc.descriptionUnder embargo until: 21.11.2018
dc.description.abstractHere 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.en_US
dc.rightsAttribution CC BY-NC-NDeng
dc.subjectCXCR4 antagonisteng
dc.titleInfluence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)en_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2017 Elsevieren_US
dc.source.journalBioorganic & Medicinal Chemistry

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