An explanation is given as to why membrane-spanning peptides must have been the first "information-rich" molecules in the development of life. These peptides are stabilised in a lipid bilayer membrane environment and they are preferentially made from the simplest, and likewise oldest, of the amino acids that survive today. Transmembrane peptides can exercise functions that are essential for biological systems such as signal transduction and material transport across membranes. More complex peptides possessing catalytic properties could later develop on either side of the membrane as independently folding functional units formed by extension of the protruding ends of the transmembrane peptides within an aqueous environment and thereby give rise to more of the functions that are necessary for life. But the membrane was the cradle for the development of the first information-rich biomolecules.
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http://dx.doi.org/10.1016/j.jtbi.2009.08.001 | DOI Listing |
J Phys Chem B
September 2024
Department of Chemical and Biological Engineering, University of Wisconsin─Madison, Madison, Wisconsin 53706, United States.
Biomolecules
August 2024
Department of Food and Drug, University of Parma, 43124 Parma, Italy.
Herein, we investigated the toxicity and membrane-permeabilizing capabilities of Lpt and Lpt-like peptides, belonging to type I toxin-antitoxin systems carried by plasmid DNA of strains. These 29 amino acid peptides are predicted to form α-helical structures with a conserved central hydrophobic sequence and differently charged hydrophilic termini. Like Lpt, the expression of Lpt-like in induced growth arrest, nucleoid condensation, and cell membrane damage, suggesting membrane interaction as the mode of action.
View Article and Find Full Text PDFMalariaworld J
August 2024
Department of Biological Sciences, The University of Texas at Dallas, Richardson, TX 75080-3021 USA.
Introduction: The cadherin G-protein coupled receptor BT-R in the mosquito is a single membrane-spanning α-helical (bitopic) protein that represents the most abundant and functionally diverse group of membrane proteins. Binding of the Cry4B toxin of subsp. (Bti) to BT-R triggers a Mg2+-dependent signalling pathway in the mosquito that involves stimulation of G protein α-subunit, which subsequently launches a coordinated signalling cascade involving Na/K-ATPase.
View Article and Find Full Text PDFTumour Virus Res
December 2024
Department of Immunobiology, University of Arizona, Tucson, AZ, USA; Department of Molecular & Cellular Biology, University of Arizona, Tucson, AZ, USA; Cancer Biology Graduate Interdisciplinary Program, University of Arizona, Tucson, AZ, USA; BIO5 Institute, University of Arizona, Tucson, AZ, USA. Electronic address:
High risk human papillomavirus (HPV) infection is responsible for 99 % of cervical cancers and 5 % of all human cancers worldwide. HPV infection requires the viral genome (vDNA) to gain access to nuclei of basal keratinocytes of epithelium. After virion endocytosis, the minor capsid protein L2 dictates the subcellular retrograde trafficking and nuclear localization of the vDNA during mitosis.
View Article and Find Full Text PDFHeart Rhythm
January 2025
Fralin Biomedical Research Institute, Virginia Polytechnic University, Roanoke, Virginia; School of Medicine, Virgina Polytechnic University, Roanoke, Virginia; Department of Biomedical Engineering and Mechanics, Virginia Polytechnic University, Blacksburg, Virginia. Electronic address:
Voltage-gated sodium channels (VGSCs) are transmembrane protein complexes that are vital to the generation and propagation of action potentials in nerve and muscle fibers. The canonical VGSC is generally conceived as a heterotrimeric complex formed by 2 classes of membrane-spanning subunit: an α-subunit (pore forming) and 2 β-subunits (non-pore forming). Na1.
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