Competition between tuftsin and HIV-1, HIV-2 envelope protein sequences. NLM AIDSLINE Important note: Information in this article was accurate in 1993. The state of the art may have changed since the publication date.

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Competition between tuftsin and HIV-1, HIV-2 envelope protein sequences.

Arch Immunol Ther Exp (Warsz). 1991;39(5-6):469-78. Unique Identifier : AIDSLINE MED/93038029
Siemion IZ; Slon J; Wieczorek Z; Institute of Chemistry, Wroclaw University.

Abstract: Syntheses of tuftsin-like partial sequences of HIV-1 and HIV-2 gp-120 proteins: Thr-Lys-Ala-Lys (I), Thr-Lys-Ala-Lys-Arg (II), Pro-Thr-Lys-Ala-Lys-Arg (III), Thr-Lys-Glu-Lys (IV), Thr-Lys-Glu-Lys-Arg (V), and Pro-Thr-Lys-Glu-Lys-Arg (VI) are described. From HIV-1 partial sequences peptide I inhibited the phagocytosis stimulating activity of tuftsin. The inhibitory potency diminished progressively for peptides II and III, in parallel to the increase of their slight phagocytosis stimulating activity. Similar results were obtained also for the fragments of the HIV-2 gp120 protein. The inhibitory activity, clearly visible for IV, diminished with peptide chain elongation. Peptides IV and VI were devoided of the phagocytosis stimulating activity while peptide V was slightly active.
Keywords: Amino Acid Sequence Animal Guinea Pigs HIV Envelope Protein gp120/*CHEMISTRY/PHARMACOLOGY HIV-1/*CHEMISTRY HIV-2/*CHEMISTRY In Vitro Molecular Sequence Data Peptide Fragments/CHEMISTRY/PHARMACOLOGY Phagocytosis/DRUG EFFECTS Sequence Homology, Amino Acid Support, Non-U.S. Gov't Tuftsin/*CHEMISTRY/PHARMACOLOGY JOURNAL ARTICLEKWDaminoacidsequenceanimalguineapigshivenvelopeproteingp120/KWDchemistry/pharmacologyhiv-1/KWDchemistryhiv-2/KWDchemistryinvitromolecularsequencedatapeptidefragments/chemistry/pharmacologyphagocytosis/drugeffectssequencehomology,aminoacidsupport,non-uKWDsKWDgov'ttuftsin/KWDchemistry/pharmacologyjournalarticle
930130
M9311137

Copyright © 1993 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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