Fluorogenic assay of alkaline phosphatase activity based on the modulation of excited-state intramolecular proton transfer

Jihye Park; Aasif Helal; Hong Seok Kim; Youngmi Kim

doi:10.1016/j.bmcl.2012.07.021

Fluorogenic assay of alkaline phosphatase activity based on the modulation of excited-state intramolecular proton transfer

Jihye Park
, Aasif Helal
, Hong Seok Kim^*
, Youngmi Kim

^*Corresponding author for this work

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

13 Scopus citations

Abstract

A new fluorogenic substrate 1, which enables the fast and quantitative analysis of alkaline phosphatase activity, has been developed. Selective enzymatic hydrolysis of 1 instantly generated fluorescent compound 2 in aqueous media, which undergo an excited-state intramolecular proton transfer process, resulting in a remarkable fluorescence turn-on signal with an unusually large Stokes shift.

Original language	English
Pages (from-to)	5541-5544
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	22
Issue number	17
DOIs	https://doi.org/10.1016/j.bmcl.2012.07.021
State	Published - 1 Sep 2012
Externally published	Yes

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. 2010-0017220 and 2010-0010070 ).

Keywords

Alkaline phosphatase
Excited-state intramolecular proton transfer
Fluorogenic assay
Inhibitor assay
Probe

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2012.07.021

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title = "Fluorogenic assay of alkaline phosphatase activity based on the modulation of excited-state intramolecular proton transfer",

abstract = "A new fluorogenic substrate 1, which enables the fast and quantitative analysis of alkaline phosphatase activity, has been developed. Selective enzymatic hydrolysis of 1 instantly generated fluorescent compound 2 in aqueous media, which undergo an excited-state intramolecular proton transfer process, resulting in a remarkable fluorescence turn-on signal with an unusually large Stokes shift.",

keywords = "Alkaline phosphatase, Excited-state intramolecular proton transfer, Fluorogenic assay, Inhibitor assay, Probe",

author = "Jihye Park and Aasif Helal and Kim, \{Hong Seok\} 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. 2010-0017220 and 2010-0010070 ). ",

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doi = "10.1016/j.bmcl.2012.07.021",

language = "English",

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pages = "5541--5544",

journal = "Bioorganic and Medicinal Chemistry Letters",

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T1 - Fluorogenic assay of alkaline phosphatase activity based on the modulation of excited-state intramolecular proton transfer

AU - Park, Jihye

AU - Helal, Aasif

AU - Kim, Hong Seok

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. 2010-0017220 and 2010-0010070 ).

PY - 2012/9/1

Y1 - 2012/9/1

N2 - A new fluorogenic substrate 1, which enables the fast and quantitative analysis of alkaline phosphatase activity, has been developed. Selective enzymatic hydrolysis of 1 instantly generated fluorescent compound 2 in aqueous media, which undergo an excited-state intramolecular proton transfer process, resulting in a remarkable fluorescence turn-on signal with an unusually large Stokes shift.

AB - A new fluorogenic substrate 1, which enables the fast and quantitative analysis of alkaline phosphatase activity, has been developed. Selective enzymatic hydrolysis of 1 instantly generated fluorescent compound 2 in aqueous media, which undergo an excited-state intramolecular proton transfer process, resulting in a remarkable fluorescence turn-on signal with an unusually large Stokes shift.

KW - Alkaline phosphatase

KW - Excited-state intramolecular proton transfer

KW - Fluorogenic assay

KW - Inhibitor assay

KW - Probe

UR - https://www.scopus.com/pages/publications/84865150754

U2 - 10.1016/j.bmcl.2012.07.021

DO - 10.1016/j.bmcl.2012.07.021

M3 - Article

C2 - 22853994

AN - SCOPUS:84865150754

SN - 0960-894X

VL - 22

SP - 5541

EP - 5544

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 17

ER -

Fluorogenic assay of alkaline phosphatase activity based on the modulation of excited-state intramolecular proton transfer

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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