PEGylation of Fluorescein by Enzyme-Catalyzed "Click" Michael Addition.
Macromol Rapid Commun
; 41(12): e2000163, 2020 Jun.
Article
en En
| MEDLINE
| ID: mdl-32431048
ABSTRACT
This paper reports the first "Click" Michael addition catalyzed by Candida antarctica lipase B (CALB) between fluorescein o-acrylate and thiol-functionalized poly(ethylene glycol)s (HS-PEG-SH, Mn = 1200 g mol-1 , D = 1.14, and Mn = 2200 g mol-1 , D = 1.09). The progress of the reactions is monitored with 1 H-NMR spectroscopy. In the absence of CALB, the reaction does not go to completion even after 18 h but completes in less than 2 min when CALB is added. Similarly, the reaction with HS-PEG-SH having Mn = 2200 g mol-1 and D = 1.09 completes in less than 2 min by CALB catalysis. The structures of the products are also confirmed by 13 C-NMR. This enzyme-catalyzed "Click" Michael addition is found to be a powerful tool to synthesize fluorescein-based polymeric conjugates for a wide variety of applications.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Polietilenglicoles
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Proteínas Fúngicas
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Fluoresceína
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Colorantes Fluorescentes
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Lipasa
Idioma:
En
Año:
2020
Tipo del documento:
Article