ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
Fibril Structure Demonstrates the Role of Iodine Labelling on a Pentapeptide Self-Assembly.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Computation meets experiment: identification of highly efficient fibrillating peptides.CrystEngComm · 2023Article
- The Antioxidant Properties of Selected Varieties of Pumpkin Fortified with Iodine in the Form of Potassium Iodide and Potassium Iodate.Foods (Basel, Switzerland) · 2023Article
- Synthesis of Amino Acids Bearing Halodifluoromethyl Moieties and Their Application to p53-Derived Peptides Binding to Mdm2/Mdm4.Drug design, development and therapy · 2023Article
- Fibril Structure Demonstrates the Role of Iodine Labelling on a Pentapeptide Self-Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
Iodination has long been employed as a successful labelling strategy to gain structural insights into proteins and other biomolecules via several techniques, including Small Angle X-ray Scattering, Inductively Coupled Plasma Mass Spectrometer (ICP-MS), and single-crystal crystallography. However, when dealing with smaller biomolecular systems, interactions driven by iodine may significantly alter their self-assembly behaviour. The engineering of amyloidogenic peptides for the development of ordered nanomaterials has greatly benefitted from this possibility. Still, to date, iodination has exclusively been applied to aromatic residues. In this work, an aliphatic bis-iodinated amino acid was synthesized and included into a custom pentapeptide, which showed enhanced fibrillogenic behaviour. Peptide single crystal X-ray structure and powder X-ray diffraction on its dried water solution demonstrated the key role of iodine atoms in promoting intermolecular interactions that drive the peptide self-assembly into amyloid fibrils. These findings enlarge the library of halogenated moieties available for directing and engineering the self-assembly of amyloidogenic peptides.
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