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PEGylation of Fluorescein by Enzyme-Catalyzed "Click" Michael Addition

PEGylation of Fluorescein by Enzyme-Catalyzed "Click" Michael Addition

Gayatri Shrikhande, Prajakatta Mulay, Judit E Puskas

Macromol Rapid Commun. 2020 Jun;41(12):e2000163.

PMID: 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 , Đ = 1.14, and Mn = 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 Mn = 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
LS775172	Poly[methyl methacrylate-co-(fluorescein O-acrylate)]			Price
LS775183	Poly(fluorescein O-acrylate)			Price

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