title: A comparative binding study of modified bovine immunodeficiency virus TAR RNA against its TAT peptide.
abstract: Besides generating novel binding peptides or small molecules to their RNA target, successful design of chemically modified RNA constructs capable of tighter binding with their binding peptides is also of significant importance. Herein, the synthesis and binding studies of a series of both wt and mutant bovine immunodeficiency virus (BIV) TAR RNA constructs against its Tat peptide are reported. Understanding the requirements that enable RNA construct binding properties, especially at the hairpin loop or internal bulge, would afford potential therapeutic approaches to control the BIV life cycle.
authors.affiliation: Department of Chemistry & Natural Sciences, York College and Graduate Center, The City University of New York (CUNY), 94-20 Guy R. Brewer Blvd., Jamaica, NY 11451, USA. tok2@llnl.gov
authors.forename: Jeffrey B-H
authors.initials: JB
authors.lastname: Tok
authors.forename: Lanrong
authors.initials: L
authors.lastname: Bi
authors.forename: Shuying
authors.initials: S
authors.lastname: Huang
mesh_terms: D000818:Animals; D002417:Cattle; D005454:Fluorescence Polarization; D015696:Gene Products, tat / Q000138:chemical synthesis / Q000737:chemistry*; D016087:Immunodeficiency Virus, Bovine / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D009154:Mutation; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012367:RNA, Viral / Q000138:chemical synthesis / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D015696:Gene Products, tat; D010446:Peptide Fragments; D012367:RNA, Viral