A metal-binding peptide appending cholic acid, Chol-MBP, formed bicelles by mixing with 1,2-dipalmitoyl--3-phosphorylcholine (DPPC). Coordination of Chol-MBP with Cu stabilized DPPC bicelles against dilution and contamination of serum proteins, enabling extended blood circulation. This study demonstrates an effective supramolecular design of phospholipid bicelles with enhanced stability useful for membrane-based biomaterials.
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http://dx.doi.org/10.1039/d2cc01058e | DOI Listing |
Proc Natl Acad Sci U S A
December 2024
Department of Chemical Engineering, The City College of New York, New York, NY 10031.
Rare earth elements (REEs) are critical materials to modern technologies. They are obtained by selective separation from mining feedstocks consisting of mixtures of their trivalent cation. We are developing an all-aqueous, bioinspired, interfacial separation using peptides as amphiphilic molecular extractants.
View Article and Find Full Text PDFJ Inorg Biochem
December 2024
Department of Chemical, Physical, Mathematical and Natural Sciences, University of Sassari, 07100 Sassari, Italy; Department of Physics and Astronomy, University of Padova, Via F. Marzolo 8, 35131 Padova, Italy.
It is a challenging task to develop uranyl-chelating agents based on peptide chemistry. A recently developed cationic dummy atom model of uranyl in conjunction with the classical molecular dynamics simulation presents a helpful utility to study the chelation of uranyl by peptides with a low computational cost. In the present study, it was used to describe the chelation of uranyl by the cyclic decapeptide with 4 Glu residues cyc-GluArgGluProGlyGluTrpGluProGly and its derivatives containing two phosphorylated serines in place of two Glu, termed pS16, pS18, pS38, and pS68.
View Article and Find Full Text PDFCommun Biol
December 2024
School of Chemistry and Chemical Engineering, University of South China, Hengyang, China.
Allosteric conformational change is an important paradigm in the regulation of protein function, which is typically triggered by the binding of small cofactors, metal ions or protein partners. Here, we found those conformational transitions can be effectively monitored by F NMR, facilitated by a site-specific F incorporation strategy at the protein C-terminus using asparaginyl endopeptidase (AEP). Three case studies show that C-terminal F-nuclei can reveal protein dynamics not only adjacent but also distal to C-terminus, including those occurring in a hemoprotein neuroglobin (Ngb), calmodulin (CaM), and a cobalt metalloregulator (CoaR) responding to both cobalt and tetrapyrrole.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
December 2024
Univ. Lille, CNRS, INSERM, Centre Hospitalier Universitaire de Lille, Institut Pasteur de Lille, U1019 - UMR 9017 - Center for Infection and Immunity of Lille, Lille F-59000, France.
J Inorg Biochem
February 2025
Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland; Chemistry and Biochemistry, Florida International University, 11200 SW 8th St, Miami, FL 33199, United States. Electronic address:
Metal ion coordination is crucial in bacterial metabolism, while divalent metal ions serve as essential cofactors for various enzymes involved in cellular processes. Therefore, bacteria have developed sophisticated regulatory mechanisms to maintain metal homeostasis. These involve protein interactions for metal ion uptake, efflux, intracellular transport, and storage.
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