The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition.
Open accessAbstract
A peptide designated DP-107 was synthesized containing amino acid residues 558-595 of the envelope glycoprotein gp160 of human immunodeficiency virus type 1 strain LAI (HIV-1LAI). Algorithms for secondary structure have predicted that this region of the envelope transmembrane protein should form an extended alpha-helix. Consistent with this prediction, analysis by circular dichroism (CD) indicated that, under physiological conditions, DP-107 is approximately 85% helical. The high degree of stable secondary structure in a synthetic peptide of this size suggests self-association typical of a coiled coil or leucine zipper. In biological assays, the peptide efficiently blocked virus-mediated cell-cell fusion processes as well as infection of peripheral blood mononuclear cells by both prototypic and primary isolates of HIV-1. A single amino acid substitution in the peptide greatly destabilized its solution structure as measured by CD and abrogated its antiviral activity. An analogue containing a terminal cysteine was oxidized to form a dimer, and this modification lowered the dose required for antiviral effect from 5 to about 1 microgram/ml. These results suggest that both oligomerization and ordered structure are necessary for biological activity. They provide insights also into the role of this region in HIV infection and the potential for development of a new class of antiviral agents.
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Cites
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Cited by
Wei, X., Decker, J. M., Liu, H., Zhang, Z., Arani, R. B., Kilby, J. M., Saag, M. S., Wu, X., Shaw, G. M., & Kappes, J. C. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.6.1896-1905.2002 · Cited by 1,569
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489
Wilen, C. B., Tilton, J. C., & Doms, R. W. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006866 · Cited by 654
Atomic structure of a thermostable subdomain of HIV-1 gp41
Tan, K., Liu, J.-H., Wang, J.-H., Shen, S., & Lu, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12303 · Cited by 532
Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes
Matthews, T., Salgo, M., Greenberg, M., Chung, J., DeMasi, R., & Bolognesi, D. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1331 · Cited by 465
Self-citation
Metadata
- Authors
- Wild, C., Oas, T., McDanal, C., Bolognesi, D., & Matthews, T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-11
- Volume
- 89
- Issue
- 21
- Pages
- 10537-10541
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2025430406
- Cited by
- 485
- References
- 16
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- green
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- Wild, C., Oas, T., McDanal, C., Bolognesi, D., & Matthews, T. (1992). A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.21.10537
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
