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Collagen Alpha 1(XI) Amino-Terminal Domain Modulates Type I Collagen Fibril Assembly.
Biochemistry
January 2025
Biomolecular Research Institute, Boise State University, 1910 University Drive, Boise, Idaho 83725, United States.
The amino-terminal domain of collagen α1(XI) plays a key role in controlling fibrillogenesis. However, the specific mechanisms through which various isoforms of collagen α1(XI) regulate this process are not fully understood. We measured the kinetics of collagen type I self-assembly in the presence of specific collagen α1(XI) isoforms.
View Article and Find Full Text PDFModular Synthesis of Anti-HER2 Dual-Drug Antibody-Drug Conjugates Demonstrating Improved Toxicity.
Bioconjug Chem
January 2025
Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112 United States.
Antibodies have gained clinical success in the last two decades for the targeted delivery of highly toxic small molecule chemotherapeutics. Yet antibody-drug conjugates (ADCs) often fail in the clinic due to the development of resistance. The delivery of two mechanistically distinct small molecule drugs on one antibody is of increasing interest to overcome these challenges with single-drug ADCs.
View Article and Find Full Text PDFNMR Spectral Editing, Water Suppression, and Dipolar Decoupling in Low-Field NMR Spectroscopy Using Optimal Control Pulses and Multiple-Pulse Sequence.
Anal Chem
January 2025
Experimental Physics III, TU Dortmund University, Dortmund 44227, Germany.
Spectral dispersion in low-field nuclear magnetic resonance (NMR) can significantly affect NMR spectral analysis, particularly when studying complex mixtures like metabolic profiling of biological samples. To address signal superposition in these spectra, we employed spectral editing with selective excitation pulses, proving it to be a suitable approach. Optimal control pulses were implemented in low-field NMR and demonstrated their capability to selectively excite and eliminate specific amino acids, such as phenylalanine and taurine, either individually or simultaneously.
View Article and Find Full Text PDFHuman recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.
Protein Sci
February 2025
Protein Biochemistry and Molecular Modeling Group, OGVFB, National Eye Institute, National Institutes of Health, Bethesda, Maryland, USA.
Oculocutaneous albinism is an autosomal recessive inherited disorder associated with mutations in the TYR gene. A single missense change in the tyrosinase (Tyr) could result in partial or complete loss of catalytic activity. The effect of two genetic mutations in the same Tyr as the molecule is less studied.
View Article and Find Full Text PDFAutomated Flow Synthesis of Artificial Heme Enzymes for Enantiodivergent Biocatalysis.
J Am Chem Soc
January 2025
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.
The remarkable efficiency with which enzymes catalyze small-molecule reactions has driven their widespread application in organic chemistry. Here, we employ automated fast-flow solid-phase synthesis to access catalytically active full-length enzymes without restrictions on the number and structure of noncanonical amino acids incorporated. We demonstrate the total syntheses of iron-dependent myoglobin (BsMb) and sperm whale myoglobin (SwMb).
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