Activity of synthetic peptides form the Tat protein of human immunodeficiency virus type 1

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 86; no. 19; pp. 7397 - 7401
• Main Authors: Frankel, AD, Biancalana, S, Hudson, D
• Format: Journal Article
• Language: English
• Published: 01.01.1989
• Subjects: human immunodeficiency virus 1
• ISSN: 0027-8424

To determine which of the 86 amino acids in the Tat protein of human immunodeficiency virus type 1 (HIV-1) are important for transactiviation, peptides from Tat were synthesized and their activity was measured in cells containing a chloramphenicol acetyltransferase reporter gene under control of the HIV long terminal repeat promoter. Although the Tat sequence contains arginine- and cysteine-rich stretches that are difficult to synthesize, it was possible to prepare pure peptides in good yield by using fluoren-9-ylmethoxycarbonyl (Fmoc) chemistry. A peptide containing residue 1-58 had 5-10% the activity of full-length Tat. Deleting 4 amino acids from the N terminus of this peptide further reduced activity, while peptides with more extensive N-terminal deletions and peptides missing the basic region at the C terminus had no detectable activity.