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  • Title: Structure-activity relationships of an anti-HIV peptide, T22.
    Author: Tamamura H, Murakami T, Masuda M, Otaka A, Takada W, Ibuka T, Nakashima H, Waki M, Matsumoto A, Yamamoto N.
    Journal: Biochem Biophys Res Commun; 1994 Dec 30; 205(3):1729-35. PubMed ID: 7811258.
    Abstract:
    T22 ([Tyr5,12,Lys7]-polyphemusin II) has been shown to have a strong anti-human immunodeficiency virus (HIV) activity comparable to that of 3'-azido-2',3'-dideoxythymidine (AZT). We studied the structure-anti-HIV activity relationships of T22 and determined the following information. The number of Arg residues in the N-terminal and C-terminal regions of T22 is closely related with anti-HIV activity. Disulfide rings, especially the major disulfide ring, are indispensable for anti-HIV activity and maintenance of the secondary structure. Between two repeats of Tyr-Arg-Lys, which are a characteristic structure contained in T22, Tyr-Arg-Lys in the N-terminal portion is more closely related with anti-HIV activity. We found some compounds having a higher selectivity index (50% cytotoxic concentration/50% effective concentration) than that of T22.
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