Adamantylglycine as a high-affinity peptide label for membrane transport monitoring and regulation

The non-canonical amino acid adamantylglycine (Ada) is introduced into peptides to allow high-affinity binding to cucurbit[7]uril (CB7). Introduction of Ada into a cell-penetrating peptide (CPP) sequence had minimal influence on the membrane transport, yet enabled up- and down-regulation of the memb...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2024-04, Vol.6 (36), p.481-4813
Main Authors: Pramod, Malavika, Alnajjar, Mohammad A, Schöpper, Sandra N, Schwarzlose, Thomas, Nau, Werner M, Hennig, Andreas
Format: Article
Language:English
Subjects:
Adamantane - analogs & derivatives
Adamantane - chemistry
Affinity
Amino acids
Biological Transport
Bridged-Ring Compounds - chemistry
Bridged-Ring Compounds - metabolism
Cell Membrane - chemistry
Cell Membrane - metabolism
Cell-Penetrating Peptides - chemistry
Cell-Penetrating Peptides - metabolism
Glycine - analogs & derivatives
Glycine - chemistry
Glycine - metabolism
Heterocyclic Compounds, 2-Ring
Humans
Imidazoles - chemistry
Imidazolidines
Macrocyclic Compounds
Membranes
Peptides
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Summary:The non-canonical amino acid adamantylglycine (Ada) is introduced into peptides to allow high-affinity binding to cucurbit[7]uril (CB7). Introduction of Ada into a cell-penetrating peptide (CPP) sequence had minimal influence on the membrane transport, yet enabled up- and down-regulation of the membrane transport activity. Adamantylglycine (Ada) is introduced into peptides for high-affinity binding to cucurbit[7]uril (CB7). Ada has minimal influence on membrane transport of cell-penetrating peptides (CPPs), but enables up- and down-regulation by CB7 binding.
ISSN:1359-7345
1364-548X
DOI:10.1039/d4cc00602j