Details
| Original language | English |
|---|---|
| Pages (from-to) | 7321-7339 |
| Number of pages | 19 |
| Journal | Chemistry - a European journal |
| Volume | 27 |
| Issue number | 26 |
| Early online date | 22 Jan 2021 |
| Publication status | Published - 6 May 2021 |
Abstract
The term “privileged structure” refers to a single molecular substructure or scaffold that can serve as a starting point for high-affinity ligands for more than one receptor type. In this report, a hitherto overlooked group of privileged substructures is addressed, namely aromatic oligoamides, for which there are natural models in the form of cystobactamids, albicidin, distamycin A, netropsin, and others. The aromatic and heteroaromatic core, together with a flexible selection of substituents, form conformationally well-defined scaffolds capable of specifically binding to conformationally well-defined regions of biomacromolecules such as helices in proteins or DNA often by acting as helices mimics themselves. As such, these aromatic oligoamides have already been employed to inhibit protein–protein and nucleic acid–protein interactions. This article is the first to bring together the scattered knowledge about aromatic oligoamides in connection with biomedical applications.
Keywords
- aromatic oligoamides, cystobactamids, DNA-binding, dystamycin, foldamers, protein–protein interactions
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- Organic Chemistry
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Chemistry - a European journal, Vol. 27, No. 26, 06.05.2021, p. 7321-7339.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Natural and Synthetic Oligoarylamides
T2 - Privileged Structures for Medical Applications
AU - Seedorf, Tim
AU - Kirschning, Andreas
AU - Solga, Danny
N1 - Funding Information: We are indebted to the BMBF (OpCyBac; grant number 16GW0219K) for funding our research on the cystobactamids. Open access funding enabled and organized by Projekt DEAL.
PY - 2021/5/6
Y1 - 2021/5/6
N2 - The term “privileged structure” refers to a single molecular substructure or scaffold that can serve as a starting point for high-affinity ligands for more than one receptor type. In this report, a hitherto overlooked group of privileged substructures is addressed, namely aromatic oligoamides, for which there are natural models in the form of cystobactamids, albicidin, distamycin A, netropsin, and others. The aromatic and heteroaromatic core, together with a flexible selection of substituents, form conformationally well-defined scaffolds capable of specifically binding to conformationally well-defined regions of biomacromolecules such as helices in proteins or DNA often by acting as helices mimics themselves. As such, these aromatic oligoamides have already been employed to inhibit protein–protein and nucleic acid–protein interactions. This article is the first to bring together the scattered knowledge about aromatic oligoamides in connection with biomedical applications.
AB - The term “privileged structure” refers to a single molecular substructure or scaffold that can serve as a starting point for high-affinity ligands for more than one receptor type. In this report, a hitherto overlooked group of privileged substructures is addressed, namely aromatic oligoamides, for which there are natural models in the form of cystobactamids, albicidin, distamycin A, netropsin, and others. The aromatic and heteroaromatic core, together with a flexible selection of substituents, form conformationally well-defined scaffolds capable of specifically binding to conformationally well-defined regions of biomacromolecules such as helices in proteins or DNA often by acting as helices mimics themselves. As such, these aromatic oligoamides have already been employed to inhibit protein–protein and nucleic acid–protein interactions. This article is the first to bring together the scattered knowledge about aromatic oligoamides in connection with biomedical applications.
KW - aromatic oligoamides
KW - cystobactamids
KW - DNA-binding
KW - dystamycin
KW - foldamers
KW - protein–protein interactions
UR - http://www.scopus.com/inward/record.url?scp=85101937378&partnerID=8YFLogxK
U2 - 10.1002/chem.202005086
DO - 10.1002/chem.202005086
M3 - Review article
C2 - 33481284
AN - SCOPUS:85101937378
VL - 27
SP - 7321
EP - 7339
JO - Chemistry - a European journal
JF - Chemistry - a European journal
SN - 0947-6539
IS - 26
ER -