https://scholars.lib.ntu.edu.tw/handle/123456789/378110
Title: | Altering the Tat-derived peptide bioactivity landscape by changing the arginine side chain length | Authors: | Wu, C.-H. Chen, Y.-P. CHUNG-YUAN MOU RICHARD PING CHENG |
Issue Date: | 2013 | Journal Volume: | 44 | Journal Issue: | 2 | Start page/Pages: | 473-480 | Source: | Amino Acids | Abstract: | Mutations of proteins with dual activities that lead to enhancement of one activity are frequently accompanied by attenuation of the other activity. However, this mutational negative trade-off phenomenon typically only involves the canonical 20 amino acids. To test the effect of non-canonical amino acids on the negative trade-off phenomenon, two bioactivities of HIV-1 Tat-derived peptides were monitored upon changing the Arg side chain length. In contrast to the expected mutational negative trade-off, shortening Arg by one methylene resulted in both higher TAR RNA binding specificity and higher cellular uptake. These results suggest that introducing previously unexploited building blocks, even if the difference is only one methylene, can alter the peptide bioactivity landscape leading to the enhancement of multiple bioactivities. ? 2012 Springer-Verlag. |
URI: | http://www.scopus.com/inward/record.url?eid=2-s2.0-84878363637&partnerID=MN8TOARS http://scholars.lib.ntu.edu.tw/handle/123456789/378110 |
DOI: | 10.1007/s00726-012-1357-0 | SDG/Keyword: | arginine; carbene; transactivator protein; amino acid sequence; anisotropy; article; binding affinity; biological activity; controlled study; fluorescence analysis; gel mobility shift assay; intracellular transport; molecular size; priority journal; RNA binding; sequence analysis; Amino Acid Sequence; Arginine; Biological Transport; Cell Line; Humans; Molecular Sequence Data; Molecular Structure; Nucleic Acid Conformation; Peptides; tat Gene Products, Human Immunodeficiency Virus; Human immunodeficiency virus 1 |
Appears in Collections: | 化學系 |
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