Interactions of AsCy3 with Cysteine-Rich Peptides

[Image: see text] There is great interest in fluorogenic compounds that tag biomolecules within cells. Biarsenicals are fluorogenic compounds that become fluorescent upon binding four proximal Cys thiols, a tetracysteine (Cys(4)) motif. This work details interactions between the biarsenical AsCy3 an...

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Autores principales: Alexander, Seth C., Schepartz, Alanna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4334252/
https://www.ncbi.nlm.nih.gov/pubmed/24999741
http://dx.doi.org/10.1021/ol501721j
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author Alexander, Seth C.
Schepartz, Alanna
author_facet Alexander, Seth C.
Schepartz, Alanna
author_sort Alexander, Seth C.
collection PubMed
description [Image: see text] There is great interest in fluorogenic compounds that tag biomolecules within cells. Biarsenicals are fluorogenic compounds that become fluorescent upon binding four proximal Cys thiols, a tetracysteine (Cys(4)) motif. This work details interactions between the biarsenical AsCy3 and Cys(4) peptides. Maximal affinity was observed when two Cys-Cys pairs were separated by at least 8 amino acids; the highest affinity ligand bound in the nanomolar concentration range (K(app) = 43 nM) and with a significant (3.2-fold) fluorescence enhancement.
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spelling pubmed-43342522015-07-07 Interactions of AsCy3 with Cysteine-Rich Peptides Alexander, Seth C. Schepartz, Alanna Org Lett [Image: see text] There is great interest in fluorogenic compounds that tag biomolecules within cells. Biarsenicals are fluorogenic compounds that become fluorescent upon binding four proximal Cys thiols, a tetracysteine (Cys(4)) motif. This work details interactions between the biarsenical AsCy3 and Cys(4) peptides. Maximal affinity was observed when two Cys-Cys pairs were separated by at least 8 amino acids; the highest affinity ligand bound in the nanomolar concentration range (K(app) = 43 nM) and with a significant (3.2-fold) fluorescence enhancement. American Chemical Society 2014-07-07 2014-07-18 /pmc/articles/PMC4334252/ /pubmed/24999741 http://dx.doi.org/10.1021/ol501721j Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Alexander, Seth C.
Schepartz, Alanna
Interactions of AsCy3 with Cysteine-Rich Peptides
title Interactions of AsCy3 with Cysteine-Rich Peptides
title_full Interactions of AsCy3 with Cysteine-Rich Peptides
title_fullStr Interactions of AsCy3 with Cysteine-Rich Peptides
title_full_unstemmed Interactions of AsCy3 with Cysteine-Rich Peptides
title_short Interactions of AsCy3 with Cysteine-Rich Peptides
title_sort interactions of ascy3 with cysteine-rich peptides
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4334252/
https://www.ncbi.nlm.nih.gov/pubmed/24999741
http://dx.doi.org/10.1021/ol501721j
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