Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition. | Zendy

Yaw-Ling Lin | Zendy; A Padmapriya | Zendy; Kathleen M. Morden | Zendy; Subashinie Jayasena | Zendy

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Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition.

Author(s) -

Yaw-Ling Lin,

A Padmapriya,

Kathleen M. Morden,

Subashinie Jayasena

Publication year - 1995

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.92.24.11044

Subject(s) - tetrapeptide , dna , peptide , in vitro , biochemistry , ligand (biochemistry) , nucleic acid , chemistry , conjugate , enzyme , microbiology and biotechnology , biology , receptor , mathematical analysis , mathematics

An in vitro selection technique was used to identify a specific high-affinity DNA ligand targeted to human neutrophil elastase (HNE). 1H NMR data and a comparative analysis of the selected sequences suggest that the DNA folds into a G-quartet structure with duplexed ends. The high-affinity binding DNA alone did not inhibit the enzymatic activity of HNE. The DNA was covalently attached to a tetrapeptide, N-methoxysuccinyl-Ala-Ala-Pro-Val, that is a weak competitive inhibitor of HNE. HNE was inhibited by this DNA-peptide conjugate nearly five orders of magnitude more effectively than by the peptide alone. These results demonstrate that in vitro-selected nucleic acids can be used as a vehicle for molecular delivery.

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