PEGylation of Fluorescein by Enzyme‐Catalyzed “Click” Michael Addition

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, M n = 1200 g mol −1 , Đ = 1.14, and M n = 2200 g mol −1 , Đ = 1.09). The progress of the reaction...

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Bibliographic Details
Published in:Macromolecular Rapid Communications
Main Authors: Shrikhande, Gayatri, Mulay, Prajakatta, Puskas, Judit E.
Other Authors: Rubber Division of the American Chemical Society, Breast Cancer Innovation Foundation
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2020
Subjects:
Materials Chemistry
Polymers and Plastics
Organic Chemistry
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1002/marc.202000163
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmarc.202000163
https://onlinelibrary.wiley.com/doi/pdf/10.1002/marc.202000163
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/marc.202000163
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Summary: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, M n = 1200 g mol −1 , Đ = 1.14, and M n = 2200 g mol −1 , Đ = 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 M n = 2200 g mol −1 and Đ = 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.

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