期刊
BIOCHEMICAL JOURNAL
卷 395, 期 -, 页码 157-163出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20051747
关键词
anthrax in vivo inhibitor; anthrax toxin; multiple antigen peptide (MAP); oedema factor; peptide stability; phage peptide
The lethal and oedema toxins produced by Bacillus anthracis, the aetiological agent of anthrax, are made by association of protective antigen with lethal and oedema factors and play a major role in the pathogenesis of anthrax. In the present paper, we describe the production of peptide-based specific inhibitors in branched form which inhibit the interaction of protective antigen with lethal and oedema factors and neutralize anthrax toxins in vitro and in vivo. Anti-protective antigen peptides were selected from a phage library by competitive panning with lethal factor. Selected 12-mer peptides were synthesized in tetra-branched form and were systematically modified to obtain peptides with higher affinity and inhibitory efficiency.
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