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| http://dx.doi.org/10.1074/jbc.A109.049221 | DOI Listing |
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Carboxy-Amidated AamAP1-Lys has Superior Conformational Flexibility and Accelerated Killing of Gram-Negative Bacteria.
Biochemistry
January 2025
Department of Biochemistry, Genetics and Microbiology, Faculty of Natural and Agricultural Sciences, University of Pretoria, Pretoria 0002, South Africa.
C-terminal amidation of antimicrobial peptides (AMPs) is a frequent minor modification used to improve antibacterial potency, commonly ascribed to increased positive charge, protection from proteases, and a stabilized secondary structure. Although the activity of AMPs is primarily associated with the ability to penetrate bacterial membranes, hitherto the effect of amidation on this interaction has not been understood in detail. Here, we show that amidation of the scorpion-derived membranolytic peptide AamAP1-Lys produces a potent analog with faster bactericidal activity, increased membrane permeabilization, and greater Gram-negative membrane penetration associated with greater conformational flexibility.
View Article and Find Full Text PDFMitochondria-targeting nanostructures from enzymatically degradable fluorescent amphiphilic polyesters.
Nanoscale
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School of Applied and Interdisciplinary Sciences, Indian Association for the Cultivation of Science (IACS), 2A and 2B Raja. S. C. Mullick Road, Jadavpur, Kolkata 700032, India.
Water-soluble π-conjugated luminescent bioprobes have been broadly used in biomedical research but are limited by the nonbiodegradability associated with their rigid C-C backbones. In the present work, we introduced three naphthalene monoimide (NMI)-functionalized amphiphilic fluorescent polyesters (P1, P2, and P3) prepared by transesterification of functional diols with an activated diester monomer of adipic acid. These polyesters featured a side-chain NMI fluorophore, imparting the required hydrophobicity for self-assembly in water and endowing the polymeric nanoassemblies with green fluorescence.
View Article and Find Full Text PDFInhibition of HMGA2 binding to AT-rich DNA by its negatively charged C-terminus.
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Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, United States.
The mammalian high mobility group protein AT-hook 2 (HMGA2) is a small DNA-binding protein that specifically targets AT-rich DNA sequences. Structurally, HMGA2 is an intrinsically disordered protein (IDP), comprising three positively charged 'AT-hooks' and a negatively charged C-terminus. HMGA2 can form homodimers through electrostatic interactions between its 'AT-hooks' and C-terminus.
View Article and Find Full Text PDFA cross-sectional study to estimate the cost of managing patients with acute on chronic liver failure at a tertiary care centre.
Med J Armed Forces India
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Senior Advisor (Medicine) & Gastroenterologist, Command Hospital (Southern Command), Pune, India.
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In Situ Analysis of Plant Tissue Using Arc iKnife Ionization Mass Spectrometry.
Anal Chem
January 2025
Cigar Technology Innovation Center of China Tobacco, Cigar Fermentation Technology Key Laboratory of China Tobacco (China Tobacco Sichuan Industrial Co., Ltd.), Chengdu 610066, People's Republic of China.
This study developed a portable arc iKnife ionization mass spectrometry (AII-MS) technique integrating a surgical knife with low-temperature arc plasma to interact with plant tissues. The thermal energy from the arc plasma induces the sputtering of water-containing plant tissues, leading to the formation of aerosols. These aerosols are then charged by plasma-generated ions, producing charged microdroplets that are ultimately detected by a mass spectrometer.
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