AEGiS-11IAC: Spectroscopic investigation of secondary structure change of a peptide from C4 region of HIV-1 gp120.

11th International AIDS Conference


Vancouver, British Columbia — July 7-12, 1996

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Spectroscopic investigation of secondary structure change of a peptide from C4 region of HIV-1 gp120.

Int Conf AIDS 1996 Jul 7-12; 11:57 (abstract no. Mo.A.1008)
Chang DK, Chien WJ, Cheng SF, Chen ST; Institute of Chemistry, Academia Sinica, Taipei, Taiwan, ROC. Fax: 886-2-783-1237. E-mail: dkc@chem.sinica.edu.tw.

OBJECTIVE: To determine the secondary structure of the C4 region of HIV-1 gp120 and its change on CD4 binding to assist vaccine and inhibitor development.

METHODS: A 44-mer peptide encompassing a CD4-binding site was synthesized and its secondary structure determined by NMR, circular dichroism (CD) spectroscopies. Binding of the 44-mer peptide to rCD4 was probed by CD and fluorescence spectroscopies.

RESULTS: Significant alpha-helix was found to exist for the 44-mer in equilibrium with beta-form and random coil. Binding of rCD4 to the peptide is indicated by a blue shift in tryptophan fluorescence; The binding also results in the enhancement of helix.

CONCLUSION: The region surrounding W411 (LAV strain) of C4 domain participates in binding to rCD4. The observed helix stabilization of the 44-mer peptide upon attachment of rCD4 may represent part of post-CD4 binding process leading to fusion between HIV and CD4-expressing cell. The results may be useful to the development of vaccines and inhibitors of gp120-CD4 binding.

Keywords: AEGIS, HIV-1, Antigens, CD4, Peptides, Circular Dichroism, Complement 4, Binding Sites, Recombinant Proteins, SK&F 106528, ICA11KWDaegis,hiv-1,antigens,cd4,peptides,circulardichroism,complement4,bindingsites,recombinantproteins,sk&f106528,ica11

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MoA1008

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