Publications by authors named "T Hogervorst"

In nature, organisms living in extreme environmental conditions produce antifreeze proteins (AFPs) that prevent the growth of ice crystals and depress the freezing point of body fluids. In this study, three different peptides derived from the N-terminal sequence of the helical type I AFP HPLC6, along with a stapled derivative produced via on-resin microwave-assisted copper(I)-catalyzed azide-alkyne cycloaddition, were conjugated to gold nanoparticles. The aim of decorating the surface of the nanoparticles with multiple copies of the peptides was to combine the ice-binding capability of the peptides with the size of a nanoparticle, thus, mimicking the protein bulkiness to enhance the peptide antifreeze activity.

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Purpose: Quality of care in total knee arthroplasty (TKA) between implants was assessed using a novel composite outcome measure, early optimal recovery (EOR), to indicate ideal clinical outcomes and minimal healthcare resource utilization.

Methods: Patients that underwent primary TKA in the study group (ATTUNE® Knee System) or control group (LCS® COMPLETE Knee System) were included in this retrospective, single-center study. EOR was defined as no complications, no readmissions, no extra outpatient visits, ≤ 48 h length of hospital stay (LOS), and restored range of motion and pain perception at 3-month follow-up.

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Introduction: Release of some of the short external rotator tendons may be needed in the direct anterior approach (DAA) for Total Hip Arthroplasty (THA). It is unknown if these tendons heal. The purpose of this prospective study is to examine short external rotator tendon healing after release and the associated effect on muscle volume.

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While most native ice-binding proteins are rigid, artificial (macro)molecular ice-binders are usually flexible. Realizing a regular array with precisely positioned ice-binding motifs on synthetic proteins, (macro)molecular ice-binders are thus challenging. Here, we exploit the predictable assembly of cyclic peptides into nanotubes as a starting point to prepare large, rigid ice-binders bearing an ice-binding site that is found in hyperactive ice-binding proteins in insects.

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Most lectins bind carbohydrate ligands with relatively low affinity, making the identification of optimal ligands challenging. Here we introduce a point accumulation in nanoscale topography (PAINT) super-resolution microscopy method to capture weak glycan-lectin interactions at the single-molecule level in living cells (Glyco-PAINT). Glyco-PAINT exploits weak and reversible sugar binding to directly achieve single-molecule detection and quantification in cells and is used to establish the relative k and k rates of a synthesized library of carbohydrate-based probes, as well as the diffusion coefficient of the receptor-sugar complex.

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