An improved fluorogenic substrate for the detection of alkaline phosphatase activity

Jeesook Park; Youngmi Kim

doi:10.1016/j.bmcl.2013.02.063

An improved fluorogenic substrate for the detection of alkaline phosphatase activity

Jeesook Park
, Youngmi Kim

Research output: Contribution to journal › Article › peer-review

35 Citations (Scopus)

Abstract

We designed a new alkaline phosphatase (ALP)-sensitive fluorogenic probe in which a self-immolative spacer group, p-hydroxybenzyl alcohol, is linked to a profluorogenic compound to improve substrate specificity. Enzymatic hydrolysis converts the fluorogenic substrate 1 to a highly fluorescent reporter 3, thus allowing for the fast and quantitative analysis of ALP activity with greatly increased affinity for the enzyme.

Original language	English
Pages (from-to)	2332-2335
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	23
Issue number	8
DOIs	https://doi.org/10.1016/j.bmcl.2013.02.063
Publication status	Published - 15 Apr 2013

Bibliographical note

Funding Information:
This research was supported by a grant from the Fundamental R&D Program for Core Technology of Materials funded by the Ministry of Knowledge Economy, Republic of Korea, and by a National Research Foundation (NRF) grant funded by the Korea government (MEST) (No. 2012R1A1A2038694).

Keywords

Alkaline phosphatase
Fluorogenic substrate
Fluorometric assay
Inhibitor assay
Turn-on probe

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10.1016/j.bmcl.2013.02.063

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abstract = "We designed a new alkaline phosphatase (ALP)-sensitive fluorogenic probe in which a self-immolative spacer group, p-hydroxybenzyl alcohol, is linked to a profluorogenic compound to improve substrate specificity. Enzymatic hydrolysis converts the fluorogenic substrate 1 to a highly fluorescent reporter 3, thus allowing for the fast and quantitative analysis of ALP activity with greatly increased affinity for the enzyme.",

keywords = "Alkaline phosphatase, Fluorogenic substrate, Fluorometric assay, Inhibitor assay, Turn-on probe",

author = "Jeesook Park and Youngmi Kim",

note = "Funding Information: This research was supported by a grant from the Fundamental R\&D Program for Core Technology of Materials funded by the Ministry of Knowledge Economy, Republic of Korea, and by a National Research Foundation (NRF) grant funded by the Korea government (MEST) (No. 2012R1A1A2038694). ",

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AU - Park, Jeesook

AU - Kim, Youngmi

N1 - Funding Information: This research was supported by a grant from the Fundamental R&D Program for Core Technology of Materials funded by the Ministry of Knowledge Economy, Republic of Korea, and by a National Research Foundation (NRF) grant funded by the Korea government (MEST) (No. 2012R1A1A2038694).

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Y1 - 2013/4/15

N2 - We designed a new alkaline phosphatase (ALP)-sensitive fluorogenic probe in which a self-immolative spacer group, p-hydroxybenzyl alcohol, is linked to a profluorogenic compound to improve substrate specificity. Enzymatic hydrolysis converts the fluorogenic substrate 1 to a highly fluorescent reporter 3, thus allowing for the fast and quantitative analysis of ALP activity with greatly increased affinity for the enzyme.

AB - We designed a new alkaline phosphatase (ALP)-sensitive fluorogenic probe in which a self-immolative spacer group, p-hydroxybenzyl alcohol, is linked to a profluorogenic compound to improve substrate specificity. Enzymatic hydrolysis converts the fluorogenic substrate 1 to a highly fluorescent reporter 3, thus allowing for the fast and quantitative analysis of ALP activity with greatly increased affinity for the enzyme.

KW - Alkaline phosphatase

KW - Fluorogenic substrate

KW - Fluorometric assay

KW - Inhibitor assay

KW - Turn-on probe

UR - https://www.scopus.com/pages/publications/84875459675

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DO - 10.1016/j.bmcl.2013.02.063

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EP - 2335

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 8

ER -

An improved fluorogenic substrate for the detection of alkaline phosphatase activity

Abstract

Bibliographical note

Keywords

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