Biomedical subjects

Prasanna G Alluri

Publications and source records attributed to Prasanna G Alluri.

5 recordsLinked to original sources

PubMed2005

Simple reporter gene-based assays for hairpin poly(amide) conjugate permeability and DNA-binding activity in living cells.

Hairpin poly(amide)s (HPs) are sequence specific DNA-binding compounds that have engendered considerable interest as potential pharmacological agents to manipulate the expression of specific genes. However, recent reports have indicated that the ability of HP conjugates to pass through cell membranes is sensitive to the cell type employed and the nature of the conjugate. Furthermore, while binding of HPs to DNA sequences in vitro is relatively well understood, packing of DNA into chromatin in living cells makes predicting the efficiency with which a given poly(amide) will bind its cognate site less certain. Previous methods to evaluate HP permeability and binding in vivo, while effective, are somewhat tedious and qualitative. We report here two related reporter gene-based assays that provide a more convenient and quantitative measure of poly(amide) permeability and DNA binding activity in living cells. We anticipate that these methods will complement existing tools and facilitate the development of HP conjugates with the desired biological activity.

Base Sequence↗

PubMed2005

A potent transactivation domain mimic with activity in living cells.

Transcriptional coactivator-binding peptoids were isolated from a large combinatorial library. One of these molecules is shown to function as a potent activation domain surrogate in mammalian cells. Up to a 900-fold increase in expression of a Gal4-responsive reporter gene is observed when a steroid conjugate of the peptoid is incubated with HeLa cells expressing a Gal4 DNA-binding domain (DBD)-glucocorticoid receptor ligand-binding domain (GRLBD) fusion protein.

Animals↗

PubMed2004

Synthetic molecules as antibody replacements.

Antibodies are by far the most versatile, valuable, and widely used protein-binding agents. They are essential tools in biological research and are increasingly being developed as therapeutic reagents. However, antibodies have a number of practical limitations, and it would be desirable in many applications to replace them with simpler, more robust synthetic molecules. Unfortunately, synthetic protein-binding agents rarely exhibit the high affinity and specificity typical of a good antibody. This article reviews efforts to overcome these limitations and to develop a facile, high-throughput methodology for the isolation of synthetic protein ligands with antibody-like binding characteristics.

Antibodies, Bispecific↗

PubMed2003

Isolation of protein ligands from large peptoid libraries.

The isolation of ligands for large numbers of proteins is an important goal in proteomics. Whereas peptide libraries are rich sources of protein-binding molecules, native peptides have certain undesirable properties, such as sensitivity to proteases that make them less than ideal for some applications. We report here the construction and characterization of large, chemically diverse combinatorial libraries of peptoids (N-substituted oligoglycines). A protocol for the isolation of specific protein-binding molecules from these libraries is described. These data suggest that peptoid libraries will prove to be inexpensive and convenient sources of protein ligands.

Amines↗

PubMed2002

Microwave-assisted solid-phase synthesis of peptoids.

Microwave irradiation reduces the reaction time for the solid-phase synthesis of peptoids. Under these conditions, coupling of each residue requires only 1 min. The purity and yields of peptoids synthesized in this way are as good as or better than those achieved using standard methods. [reaction: see text]

Amino Acid Sequence↗