Thomas Heerde

ORCID: 0000-0002-2142-3120
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About
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Research Areas
  • Protein Structure and Dynamics
  • Alzheimer's disease research and treatments
  • Nanoplatforms for cancer theranostics
  • Photodynamic Therapy Research Studies
  • Antimicrobial Peptides and Activities
  • Supramolecular Self-Assembly in Materials
  • Enzyme Structure and Function
  • HIV Research and Treatment
  • Cancer Research and Treatments
  • Prion Diseases and Protein Misfolding
  • Antifungal resistance and susceptibility
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Bacterial biofilms and quorum sensing

Universität Ulm
2020-2023

Abstract Several studies showed that seeding of solutions monomeric fibril proteins with ex vivo amyloid fibrils accelerated the kinetics formation in vitro but did not necessarily replicate seed structure. In this research we use cryo-electron microscopy and other methods to analyze ability serum A (SAA)1.1-derived fibrils, purified from systemic AA amyloidosis tissue, recombinant SAA1.1 protein. We show 98% seeded remodel full structure main morphology, which used for seeding, while they...

10.1038/s41467-021-27688-5 article EN cc-by Nature Communications 2022-01-10

Abstract Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness amyloids with ability to catalyze a certain reaction. In this study we used cryo-electron microcopy analyze fibril structure catalytic center hydrolyze ester bonds. Our findings show polymorphic consist similarly structured, zipper-like building blocks mated cross-β sheets. These define core, which is decorated by peripheral leaflet peptide molecules....

10.1038/s41598-023-30711-y article EN cc-by Scientific Reports 2023-03-11

Abstract Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy analyze structure a biotechnologically engineered peptide fibril that enhances infectivity. Our findings show undergoes time-dependent morphological maturation into polymorphic amyloid structures. The consist mated cross-β sheets interact by hydrophobic residues amphipathic fibril-forming peptide....

10.1038/s41467-023-40042-1 article EN cc-by Nature Communications 2023-07-18

Abstract The pathogenic yeast Candida auris has received increasing attention due to its ability cause fatal infections, resistance toward important fungicides, and persist on surfaces including medical devices in hospitals. To brace health care systems for this considerable risk, alternative therapeutic approaches such as antifungal peptides are urgently needed. In clinical wound care, a significant focus been directed novel surgical (wound) dressings first defense lines against C. ....

10.1002/mabi.202000005 article EN cc-by-nc-nd Macromolecular Bioscience 2020-02-27

Azulitox as a new fusion polypeptide with cancer cell specificity and phototoxicity was generated is composed of photosensitizer domain the cell-penetrating peptide P28. The (EcFbFP) derived from bacterial blue-light receptor, which belongs to family light-oxygen-voltage proteins produces reactive oxygen species (ROS) upon excitation. P28 cupredoxin protein azurin that known specifically penetrate cells bind tumor suppressor p53. We show directs translocates fused into cells. Under...

10.1021/acs.biomac.0c01216 article EN Biomacromolecules 2020-11-03
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