JBC INTERFERin siRNA transfection reagent

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Volume 271, Number 23, Issue of June 7, 1996 pp. 13829-13833
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Contribution of Arginine Residues in the RP135 Peptide Derived from the V3 Loop of gp120 to Its Interaction with the Fv Fragment of the 0.5beta HIV-1 Neutralizing Antibody

(Received for publication, January 19, 1996, and in revised form, March 8, 1996)

Gabriel A. Faiman , Rina Levy , Jacob Anglister and Amnon Horovitz

From the Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel

The construction, expression, and purification of an active Fv fragment of the 0.5beta monoclonal human immunodeficiency virus type 1 (HIV-1) neutralizing antibody is reported. The interaction between the Fv fragment and the RP135 peptide derived from the V3 loop of gp120 from HIV-1IIIB was studied by varying the salt concentration and by mutating arginine residues in the peptide. The mutations R4A, R8A and R11A (which correspond to residues 311, 315, and 318 in gp120 of HIV-1IIIB) reduce the binding free energy by 0.22 (± 0.20), 4.32 (± 0.16), and 1.58 (± 0.17) kcal mol-1, respectively. The salt-dependent components of their contributions to binding are 0.02 (± 0.22), -0.55 (± 0.18), and -0.97 (± 0.19) kcal mol-1, respectively. The magnitudes of the mutational effects and the extent of shielding by 1 M NaCl suggest that Arg-8 is involved in a buried salt bridge in the peptide-Fv fragment complex, whereas Arg-11 is involved in a more solvent-exposed electrostatic interaction.


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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.