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ISEV2026 Abstract Book

Journal of Extracellular Vesicles, Volume 15, Issue S1, June 2026.
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Molecular dynamics of HIV‐1 protease

Proteins: Structure, Function, and Bioinformatics, 1992
AbstractMolecular dynamics simulations have been carried out based on the GROMOS force field on the aspartyl protease (PR) of the human immunodeficiency virus HIV‐1. The principal simulation treats the HIV‐1 PR dimer and 6990 water molecules in a hexagonal prism cell under periodic bundary conditions and was carried out for a trajectory of 100 psec ...
W E, Harte, S, Swaminathan, D L, Beveridge   +2 more
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Flexibility and function in HIV-1 protease

Nature Structural & Molecular Biology, 1995
HIV protease is a homodimeric protein whose activity is essential to viral function. We have investigated the molecular dynamics of the HIV protease, thought to be important for proteinase function, bound to high affinity inhibitors using NMR techniques.
Nicholson, L. K., Yamazaki, T., Torchia, D. A., Grzesiek, S., Bax, A., Stahl, S. J., Kaufman, J. D., Wingfield, P. T., Lam, P. Y. S., Jadhav, P. K., Hodge, C. N., Domaille, P. J., Chang, C. H.   +12 more
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Affinity purification of the HIV-1 protease

Biochemical and Biophysical Research Communications, 1989
An inhibitor of the HIV-1 protease has been employed in the generation of a resin which allows the rapid purification of this enzyme. A peptide substrate analogue, H2N-Ser-Gln-Asn-(Phe-psi[CH2N]-Pro)-Ile-Val-Gln-OH, was coupled to agarose resin. The HIV-1 protease was expressed in E.
J C, Heimbach, V M, Garsky, S R, Michelson, R A, Dixon, I S, Sigal, P L, Darke   +5 more
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HIV-1 protease inhibitors in development

Expert Opinion on Investigational Drugs, 2002
Several pharmaceutical companies have developed an increasing number of second generation protease inhibitors (PI) during the last few years. Many of these compounds have been in preclinical trials and some are now in clinical use. All drugs in this category have been designed to be well absorbed and overcome the crucial problem of cross-resistance ...
S. Rusconi, S. La Seta Catamancio
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Dimerization Inhibitors of HIV-1 Protease

Biological Chemistry, 2002
By targeting the highly conserved antiparallel beta-sheet formed by the interdigitation of the N- and C-terminal strands of each monomer, dimerization inhibitors of HIV-1 protease may be useful to overcome the drug resistance observed with current active-site directed antiproteases.
Nicole, Boggetto, Michèle, Reboud-Ravaux   +1 more
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Inhibitors of HIV-1 Protease

Journal of Enzyme Inhibition, 1992
The human immunodeficiency virus (HIV), the etiological agent for the acquired immune deficiency syndrome (AIDS), is a retrovirus which makes use of a virally-encoded aspartic protease to perform specific proteolytic processing of two of its gene products in order to form active enzymes and structural proteins within the mature virion.
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A radiometric assay for HIV-1 protease

Analytical Biochemistry, 1990
A rapid, high-throughput radiometric assay for HIV-1 protease has been developed using ion-exchange chromatography performed in 96-well filtration plates. The assay monitors the activity of the HIV-1 protease on the radiolabeled form of a heptapeptide substrate, [tyrosyl-3,5-3H]Ac-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2, which is based on the p17-p24 cleavage ...
L J, Hyland, B D, Dayton, M L, Moore, A Y, Shu, J R, Heys, T D, Meek   +5 more
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Purification of Recombinant HIV-1 Protease

Preparative Biochemistry, 1991
A method is described to purify recombinant HIV-1 protease from soluble extracts of Escherichia coli. The isolation involves QAE-Sepharose anion exchange chromatography, hexyl agarose hydrophobic interaction chromatography, MonoS cation exchange chromatography, and Superose 6 size exclusion chromatography.
N, Margolin, A, Dee, M, Lai, C J, Vlahos
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