Versatile symport transporters based on cyclic peptide dimers.


Journal

Chemical communications (Cambridge, England)
ISSN: 1364-548X
Titre abrégé: Chem Commun (Camb)
Pays: England
ID NLM: 9610838

Informations de publication

Date de publication:
17 Dec 2019
Historique:
pubmed: 27 11 2019
medline: 28 12 2019
entrez: 27 11 2019
Statut: ppublish

Résumé

We present the synthesis and transmembrane transport properties of a new family of tris-pyridine-decorated cyclic peptides. These molecules are designed to self-assemble into dimeric shuttles in nonpolar media, which act as symport ionophores in which, apparently, the tris-pyridine scaffold complexes both cations and anions with high potency and efficacy.

Identifiants

pubmed: 31768506
doi: 10.1039/c9cc06644f
doi:

Substances chimiques

Chlorides 0
Ionophores 0
Lipid Bilayers 0
Peptides, Cyclic 0
Pyridines 0
Unilamellar Liposomes 0
Calcium SY7Q814VUP

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

46-49

Auteurs

Alberto Fuertes (A)

Singular Research Centre in Chemical Biology and Molecular Materials, (CIQUS), Organic Chemistry Department, University of Santiago de Compostela (USC), 15782, Santiago de Compostela, Spain. manuel.amorin@usc.es juanr.granja@usc.es.

Articles similaires

Aspergillus Hydrogen-Ion Concentration Coculture Techniques Secondary Metabolism Streptomyces rimosus
Psoriasis Humans Magnesium Zinc Trace Elements

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Humans Vitiligo Male Female Adult

Classifications MeSH