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Biology subjects

Ryu, W. H.

Publications and source records attributed to Ryu, W. H..

2 recordsLinked to original sources

Design, synthesis and profiling of highly potent antivirals targeting emerging drug-resistant HIV-1 variants

AbstractLenacapavir (LEN), the first-in-class HIV capsid inhibitor (CAI), is approved by FDA as a long acting injectable (LAI) for both treatment and pre-exposure prophylaxis (PrEP). Despite its exceptional potency and long pharmacokinetics (PK), a few major resistant mutations have been selected in LEN-treated patients, underscoring the need to develop second-generation LEN analogs to mitigate resistance. Particularly, the M66I mutation confers an extraordinarily high-level LEN resistance, essentially abrogating LEN potency. In this work, we have designed and synthesized LEN analogs featuring a cycloalkyl R2 in subunit B drastically different from known analogs. Against wild-type HIV-1, the potency of our analog 3 (EC50 = 0.073 nM) was 2.6-fold higher than LEN (EC50 = 0.19 nM). More importantly, against the M66I mutant, 3 (EC50 = 5.8 nM) was decisively more potent than LEN (EC50 > 15 M) or any known analogs. We have also shown that the size of the R2 cycloalkyl ring is a major pharmacophore factor as a smaller (cyclopropyl, analog 1) or bigger (cyclohexyl, analog 4) ring confers weaker antiviral potency against both WT HIV-1 and M66I. The vastly improved profile of our lead 3 against M66I was confirmed in the target binding thermal shift assay. These results strongly validate our design and may represent a breakthrough in LEN-based HIV therapy and prophylaxis.

microbiology↗

Design of facilitated dissociation enables control over cytokine signaling duration

Protein design has focused primarily on the design of ground states, ensuring they are sufficiently low energy to be highly populated1. Designing the kinetics and dynamics of a system requires, in addition, the design of excited states that are traversed in transitions from one low-lying state to another2,3. This is a challenging task as such states must be sufficiently strained to be poorly populated, but not so strained that they are not populated at all, and because protein design methods have generally focused on creating near-ideal structures4-7. Here we describe a general approach for designing systems which use an induced-fit power stroke8 to generate a structurally frustrated9 and strained excited state, allosterically driving protein complex dissociation. X-ray crystallography, double electron-electron resonance spectroscopy, and kinetic binding measurements demonstrate that incorporating excited states enables design of effector-induced increases in dissociation rates as high as 6000-fold. We highlight the power of this approach by designing cytokine mimics which can be dissociated within seconds from their receptors.

biochemistry↗