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. 1990 Jun;64(6):3074–3077. doi: 10.1128/jvi.64.6.3074-3077.1990

Chemical synthesis of biologically active tat trans-activating protein of human immunodeficiency virus type 1.

R Chun 1, C G Glabe 1, H Fan 1
PMCID: PMC249495  PMID: 2186178

Abstract

Full-length (86-residue) polypeptide corresponding to the human immunodeficiency virus type 1 tat trans-activating protein was chemically synthesized on a semiautomated apparatus, using an Fmoc amino acid continuous-flow strategy. The bulk material was relatively homogeneous, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing, and it showed trans-activating activity when scrape loaded into cells containing a human immunodeficiency virus long terminal repeat-chloramphenicol acetyl-transferase reporter plasmid. Reverse-phase high-pressure liquid chromatography yielded a rather broad elution profile, and assays across the column for biological activity indicated a sharper peak. Thus, high-pressure liquid chromatography provided for enrichment of biological activity. Fast atom bombardment-mass spectrometry of tryptic digests of synthetic tat identified several of the predicted tryptic peptides, consistent with accurate chemical synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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