Identification of the amino acid-AZT-phosphoramidase by affinity T7 phage display selection.

Bioorg Med Chem Lett

Department of Medicinal Chemistry, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA.

Published: November 2009

AI Article Synopsis

  • A CEM cell cDNA T7 phage display library was created for screening enzymes that activate phosphoramidate prodrugs of AZT monophosphate.
  • Although hHint 1 was found to be an important enzyme, its efficiency is lower than that of ribonucleotide-based phosphoramidates in activating these prodrugs.
  • hHint 1 is suggested to play a significant role as the intracellular enzyme that converts these prodrug forms into their active counterparts.

Article Abstract

A CEM cell cDNA T7 phage display library was prepared and used to screen for activating enzymes of phosphoramidate prodrugs of AZT monophosphate. Although, inefficient compared to ribonucleotide based phosphoramidates, hHint 1 was identified as the likely intracellular pronucleotide activating enzyme.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bmcl.2009.09.067DOI Listing

Publication Analysis

Top Keywords

phage display
8
identification amino
4
amino acid-azt-phosphoramidase
4
acid-azt-phosphoramidase affinity
4
affinity phage
4
display selection
4
selection cem
4
cem cell
4
cell cdna
4
cdna phage
4

Similar Publications

Development of targeted antimicrobial peptides for Escherichia coli: Combining phage display and rational design for food safety application.

Food Chem

December 2024

Laboratory of Molecular Nutrition and Immunity, College of Animal Science and Technology, Northeast Agricultural University, Harbin, PR China. Electronic address:

The growing demand for minimally processed foods has heightened the risk of pathogenic contamination. Balancing antimicrobial efficacy with the preservation of probiotic activity remains a significant challenge. In this study, we employed phage display peptide library screening, combined with next-generation sequencing to identify the HIMPIQA domain, which selectively targets pathogenic Escherichia coli (E.

View Article and Find Full Text PDF

FOXM1 is the "Achilles' heel" of cancers and hence the potential therapeutic target for anticancer drug discovery. In this work, we selected high affinity peptides against the protein of human DNA binding domain of FOXM1 (FOXM1-DBD) from the disulfide-constrained, phage displayed random cyclic heptapeptide library Ph.D.

View Article and Find Full Text PDF

Background: Anti- Aβ monoclonal antibodies are the first FDA-approved treatments for AD that slow cognitive decline and lower Aβ plaques. Our goal is to identify the epitope specificities of antibodies in human blood that are associated with AD and NC and determine the predicted protein targets of these antibodies.

Method: 101 AD (MMSE < 27) and 98 NC (MMSE > 27) serum samples were obtained from the UCI tissue repository.

View Article and Find Full Text PDF

Background: Mature T-cell neoplasms arise from the neoplastic transformation of a single T lymphocyte, and all cells in a neoplastic clone share the same V segment in the beta chain of the T-cell receptor (TCR). These segments may represent an innovative target for the development of targeted therapies.

Methods: A specific V segment of the TCR beta chain (TRBV5-1) was analyzed using bioinformatic tools, identifying three potential antigenic peptides.

View Article and Find Full Text PDF

Screening and identification of vascular endothelial cell targeting peptide in gastric cancer through novel integrated in vitro and in vivo strategy.

BMC Cancer

December 2024

Department of Radiation Oncology, Nanfang Hospital, Southern Medical University, 1838 North Guangzhou Avenue, Guangzhou, 510515, Guangdong, P.R. China.

Purpose: Antiangiogenesis therapy has become a hot field in cancer research. Given that tumor blood vessels often express specific markers related to angiogenesis, the study of these heterogeneous molecules in different tumor vessels holds promise for advancing anti-angiogenic therapy. Previously using phage display technology, we identified a targeting peptide named GX1 homing to gastric cancer vessels for the first time.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!