Polydopamine Nanobowl-Armoured Perfluorocarbon Emulsions: Tracking Thermal- and Photothermal-Induced Phase Change through Neutron Scattering.

Anisotropic polydopamine nanobowls (PDA NBs) show significant promise in biomedicine, distinguished by their unique optical properties and superior cellular uptake compared to spherical nanoparticles. This study presents a novel approach for creating multistimuli-activated PDA NB-armored emulsions, encapsulating perfluorohexane (NB-H) and perfluoropentane (NB-P) cores, with applications in controlled delivery and ultrasound imaging. Thermal and photothermal activation induced distinct responses in the emulsions, as evidenced by optical microscopy and thermogravimetric analysis.

Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution.

The human immunodeficiency virus type 1 envelope glycoprotein (Env) complex is the principal focus of neutralizing antibody-based vaccines. The functional Env complex is a trimer consisting of six individual subunits: three gp120 molecules and three gp41 molecules. The individual subunits have proven unsuccessful as vaccines presumably because they do not resemble the functional Env complex.

Mechanistic studies of a T20-dependent human immunodeficiency virus type 1 variant.

We previously described a T20-dependent human immunodeficiency virus type 1 variant from a patient on T20 therapy. This virus carries two mutations in the gp41 domain of the envelope protein (Env) that was proposed to undergo a premature conformational switch to the 6-helix bundle structure. The T20 peptide can rescue this hyperfusogenic Env protein by preventing the premature switch and preserving an earlier prefusion conformation, thus restoring virus infectivity and replication.

HIV-1 drug-resistance and drug-dependence.

In this review, we will describe several recent HIV-1 studies in which a drug-dependent virus variant was selected. A common evolutionary route to the drug-dependence phenotype is proposed. First, the selection of a drug-resistance mutation that also affects the function of the targeted viral protein.

Second site escape of a T20-dependent HIV-1 variant by a single amino acid change in the CD4 binding region of the envelope glycoprotein.

Background: We previously described the selection of a T20-dependent human immunodeficiency virus type-1 (HIV-1) variant in a patient on T20 therapy. The fusion inhibitor T20 targets the viral envelope (Env) protein by blocking a conformational switch that is critical for viral entry into the host cell. T20-dependent viral entry is the result of 2 mutations in Env (GIA-SKY), creating a protein that undergoes a premature conformational switch, and the presence of T20 prevents this premature switch and rescues viral entry.

On the influence of oxygen and cell concentration in an SFPR whole cell biocatalytic Baeyer-Villiger oxidation process.

Efficient whole cell biotransformations, in particular microbial whole cell Baeyer-Villiger oxidation with molecular oxygen, demand comprehension and optimization of the process details involved. Optimal provision of oxygen and control of bioprocess parameters are pivotal for their success. The interrelation of cell density and oxygen supply in an in situ substrate feeding and product removal (SFPR) whole cell Baeyer-Villiger oxidation process was investigated in detail.

Improving the safety of a conditional-live human immunodeficiency virus type 1 vaccine by controlling both gene expression and cell entry.

Live attenuated human immunodeficiency virus type 1 (HIV-1) vaccines are considered unsafe because faster-replicating pathogenic virus variants may evolve after vaccination. We previously presented a conditional-live HIV-1 variant of which replication can be switched off as an alternative vaccination strategy. To improve the safety of such a vaccine, we constructed a new HIV-1 variant that depends not only on doxycycline for gene expression but also on the T20 peptide for cell entry.

Emergence of a drug-dependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor.

The fusion inhibitor T20 belongs to a new class of anti-human immunodeficiency virus type 1 (HIV-1) drugs designed to block entry of the virus into the host cell. However, the success of T20 has met with the inevitable emergence of drug-resistant HIV-1 variants. We describe an evolutionary pathway taken by HIV-1 to escape from the selective pressure of T20 in a treated patient.