Highly Stable Meldrum's Acid Derivatives for Irreversible Aqueous Covalent Modification of Amines

Garrett J. Davis; Holly A. Sofka; John C. Jewett

doi:10.1021/acs.orglett.0c00597

Highly Stable Meldrum's Acid Derivatives for Irreversible Aqueous Covalent Modification of Amines

Garrett J. Davis
, Holly A. Sofka
, John C. Jewett

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

12 Scopus citations

Abstract

This work describes the development of a highly stable and pH-responsive probe for lysine modification. The scaffold has marked stability in the presence of several biological nucleophiles and across a wide pH range (2-12). Several functional analogs showed robust labeling of a protein at pH > 9. Taken together, our system displays versatility and can be easily adapted for variety of applications, while demonstrating stability suitable for a wide range of biologically compatible systems.

Original language	English (US)
Pages (from-to)	2626-2629
Number of pages	4
Journal	Organic Letters
Volume	22
Issue number	7
DOIs	https://doi.org/10.1021/acs.orglett.0c00597
State	Published - Apr 3 2020

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/acs.orglett.0c00597

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title = "Highly Stable Meldrum's Acid Derivatives for Irreversible Aqueous Covalent Modification of Amines",

abstract = "This work describes the development of a highly stable and pH-responsive probe for lysine modification. The scaffold has marked stability in the presence of several biological nucleophiles and across a wide pH range (2-12). Several functional analogs showed robust labeling of a protein at pH > 9. Taken together, our system displays versatility and can be easily adapted for variety of applications, while demonstrating stability suitable for a wide range of biologically compatible systems.",

author = "Davis, \{Garrett J.\} and Sofka, \{Holly A.\} and Jewett, \{John C.\}",

note = "Funding Information: This work was supported in part by a NSF-Career Award to J.C.J. (CHE-1552568). H.A.S. received support from Graduate Access Fellowship and NIH Training Grant (T32 GM008804). All FTIR spectra were collected in the W. M. Keck Center for Nano-Scale Imaging in the Department of Chemistry and Biochemistry at the University of Arizona, purchased with support by the Arizona Technology and Research Initiative Fund (A.R.S.§15-1648). We also thank the NSF for a departmental instrumentation grant for the NMR facility (CHE-0840336). Publisher Copyright: Copyright {\textcopyright} 2020 American Chemical Society.",

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doi = "10.1021/acs.orglett.0c00597",

language = "English (US)",

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AU - Davis, Garrett J.

AU - Sofka, Holly A.

AU - Jewett, John C.

N1 - Funding Information: This work was supported in part by a NSF-Career Award to J.C.J. (CHE-1552568). H.A.S. received support from Graduate Access Fellowship and NIH Training Grant (T32 GM008804). All FTIR spectra were collected in the W. M. Keck Center for Nano-Scale Imaging in the Department of Chemistry and Biochemistry at the University of Arizona, purchased with support by the Arizona Technology and Research Initiative Fund (A.R.S.§15-1648). We also thank the NSF for a departmental instrumentation grant for the NMR facility (CHE-0840336). Publisher Copyright: Copyright © 2020 American Chemical Society.

PY - 2020/4/3

Y1 - 2020/4/3

N2 - This work describes the development of a highly stable and pH-responsive probe for lysine modification. The scaffold has marked stability in the presence of several biological nucleophiles and across a wide pH range (2-12). Several functional analogs showed robust labeling of a protein at pH > 9. Taken together, our system displays versatility and can be easily adapted for variety of applications, while demonstrating stability suitable for a wide range of biologically compatible systems.

AB - This work describes the development of a highly stable and pH-responsive probe for lysine modification. The scaffold has marked stability in the presence of several biological nucleophiles and across a wide pH range (2-12). Several functional analogs showed robust labeling of a protein at pH > 9. Taken together, our system displays versatility and can be easily adapted for variety of applications, while demonstrating stability suitable for a wide range of biologically compatible systems.

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JO - Organic Letters

JF - Organic Letters

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ER -

Highly Stable Meldrum's Acid Derivatives for Irreversible Aqueous Covalent Modification of Amines

Abstract

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