Unknown

Dataset Information

0

Synthesis of sequence-specific DNA-protein conjugates via a reductive amination strategy.


ABSTRACT: DNA-protein cross-links (DPCs) are ubiquitous, structurally diverse DNA lesions formed upon exposure to bis-electrophiles, transition metals, UV light, and reactive oxygen species. Because of their superbulky, helix distorting nature, DPCs interfere with DNA replication, transcription, and repair, potentially contributing to mutagenesis and carcinogenesis. However, the biological implications of DPC lesions have not been fully elucidated due to the difficulty in generating site-specific DNA substrates representative of DPC lesions formed in vivo. In the present study, a novel approach involving postsynthetic reductive amination has been developed to prepare a range of hydrolytically stable lesions structurally mimicking the DPCs produced between the N7 position of guanine in DNA and basic lysine or arginine side chains of proteins and peptides.

SUBMITTER: Wickramaratne S 

PROVIDER: S-EPMC3799944 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Synthesis of sequence-specific DNA-protein conjugates via a reductive amination strategy.

Wickramaratne Susith S   Mukherjee Shivam S   Villalta Peter W PW   Schärer Orlando D OD   Tretyakova Natalia Y NY  

Bioconjugate chemistry 20130816 9


DNA-protein cross-links (DPCs) are ubiquitous, structurally diverse DNA lesions formed upon exposure to bis-electrophiles, transition metals, UV light, and reactive oxygen species. Because of their superbulky, helix distorting nature, DPCs interfere with DNA replication, transcription, and repair, potentially contributing to mutagenesis and carcinogenesis. However, the biological implications of DPC lesions have not been fully elucidated due to the difficulty in generating site-specific DNA subs  ...[more]

Similar Datasets

| S-EPMC5864842 | biostudies-other
| S-EPMC2713763 | biostudies-literature
| S-EPMC7064911 | biostudies-literature
| S-EPMC8650211 | biostudies-literature
| S-EPMC11347174 | biostudies-literature
| S-EPMC4136702 | biostudies-literature
| S-EPMC8251741 | biostudies-literature
| S-EPMC6385856 | biostudies-other
| S-EPMC2441794 | biostudies-literature
| S-EPMC8048798 | biostudies-literature