The combination of circular CT with a helical trajectory segment results in a mathematically complete data set. We present a reconstruction algorithm which is mathematically exact and of the filtered back-projection type. The algorithm ensures that only Radon planes which are not covered along the circle are taken into account, when data from the helical segment are back-projected. Therefore, the helical segment contributes only to low-frequency parts of trans-axial slices. Data along the helix can be obtained with a very low acquisition dose.
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http://dx.doi.org/10.1088/0031-9155/52/1/008 | DOI Listing |
J Med Chem
December 2024
Univ. Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, IECB, F-33607 Pessac, France.
Combining helical foldamers with α-peptides can produce α-helix mimetics with a reduced peptide character and enhanced resistance to proteolysis. Previously, we engineered a hybrid peptide-oligourea sequence replicating the N-terminal α-helical domain of p53 to achieve high affinity binding to hDM2. Here, we further advance this strategy by combining the foldamer approach with side chain cross-linking to create more constrained cell-permeable inhibitors capable of effectively engaging the target within cells.
View Article and Find Full Text PDFJ Med Chem
December 2024
Biochemistry and Structural Biology Division, CSIR-Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, India.
The quest for new approaches for generating novel bioactive designer proteins/peptides has continued with their success in various biomedical applications. Previously, we designed a 14-mer α-helical peptide with antimicrobial and antimycobacterial activities by employing a tandem repeat of the 7-mer, "KVLGRLV" human chemerin segment. Herein, we devised a new method of "sliding framework" with this segment to create amino acid scaffolds of varying sizes and sequences and explored the design of a peptide library with antibacterial and antimycobacterial activities.
View Article and Find Full Text PDFJ Phys Chem B
December 2024
Simons Centre for the Study of Living Machines, National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India.
The homotrimeric SARS-CoV-2 spike protein enables viral infection by undergoing a large conformational transition, which facilitates the fusion of the viral envelope with the host cell membrane. The spike protein is anchored to the SARS-CoV-2 envelope by its transmembrane domain (TMD), composed of three TM helices, each contributed by one of the protomers of spike. Although the TMD is known to be important for viral fusion, whether it is a passive anchor of the spike or actively promotes fusion remains unknown.
View Article and Find Full Text PDFNucleic Acids Res
December 2024
Univ. Grenoble Alpes, CNRS, CEA, IBS, 71 avenue des Martyrs, F-38000 Grenoble, France.
Influenza A viruses are responsible for human seasonal epidemics and severe animal pandemics with a risk of zoonotic transmission to humans. The viral segmented RNA genome is encapsidated by nucleoproteins (NP) and attached to the heterotrimeric polymerase, forming the viral ribonucleoproteins (vRNPs). Flexible helical vRNPs are central for viral transcription and replication.
View Article and Find Full Text PDFChemistry
December 2024
Key Laboratory of Synthetic and Self-Assembly Chemistry for Organic Functional Molecules, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai, 200032, China.
In this study, several hydrogen-bonded arylamide foldamers (compounds 1-5) with the same degree of polymerization were designed and synthesized. The polyfluoroiodobenzene or iodoethynyl polyfluoroiodobenzene segment was modified as a halogen donor at the end of the monomer, and pyridine or pyridine oxynitride served as the corresponding halogen acceptor segment. The crystal structure of compound 1 indicates that the supramolecular double helices were constructed by stacking a P helix and an M helix in an antiparallel manner in the direction of intermolecular I⋅⋅⋅O-N halogen bonding.
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