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Puckering effects of 4-hy-droxy-l-proline isomers on the conformation of ornithine-free Gramicidin S.
Acta Crystallogr E Crystallogr Commun
September 2024
Osaka Medical and Pharmaceutical University, 4-20-1 Nasahara, Takatsuki, Osaka 590-1094, Japan.
The cyclic peptide (Val-Leu-Leu-d-Phe-Pro) (peptide ) was specifically designed for structural chemistry investigations, drawing inspiration from Gramicidin S (GS). Previous studies have shown that Pro residues within adopt a down-puckering conformation of the pyrrolidine ring. By incorporating fluoride-Pro with 4-/-isomers into , an up-puckering conformation was successfully induced.
View Article and Find Full Text PDFModifying Membranotropic Action of Antimicrobial Peptide Gramicidin S by Star-like Polyacrylamide and Lipid Composition of Nanocontainers.
Int J Mol Sci
August 2024
Department of Life Sciences and Systems Biology, University of Turin, Via Accademia Albertina 13, 10123 Turin, Italy.
Gramicidin S (GS), one of the first discovered antimicrobial peptides, still shows strong antibiotic activity after decades of clinical use, with no evidence of resistance. The relatively high hemolytic activity and narrow therapeutic window of GS limit its use in topical applications. Encapsulation and targeted delivery may be the way to develop the internal administration of this drug.
View Article and Find Full Text PDFAlignment of lyotropic liquid crystals using magnetic nanoparticles improves ionic transport through built-in peptide ion channels.
J Colloid Interface Sci
November 2024
Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland; Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02089 Warsaw, Poland. Electronic address:
Hypothesis: We hypothesize that simultaneous incorporation of ion channel peptides (in this case, potassium channel as a model) and hydrophobic magnetite FeO nanoparticles (hFeONPs) within lipidic hexagonal mesophases, and aligning them using an external magnetic field can significantly enhance ion transport through lipid membranes.
Experiments: In this study, we successfully characterized the incorporation of gramicidin membrane ion channels and hFeONPs in the lipidic hexagonal structure using SAXS and cryo-TEM methods. Additionally, we thoroughly investigated the conductive characteristics of freestanding films of lipidic hexagonal mesophases, both with and without gramicidin potassium channels, utilizing a range of electrochemical techniques, including impedance spectroscopy, normal pulse voltammetry, and chronoamperometry.
Formation of sparsely tethered bilayer lipid membrane on a biodegradable self-assembled monolayer of poly(lactic acid).
Bioelectrochemistry
October 2024
IMEM-BRT Group, Departament d'Enginyeria Química, EEBE, Universitat Politècnica de Catalunya, C/ Eduard Maristany, 10-14, Ed. I, 2nd Floor, 08019 Barcelona, Spain; Barcelona Research Center in Multiscale Science and Engineering, EEBE, Universitat Politècnica de Catalunya, C/ Eduard Maristany, 10-14, Basement S-1, 08019 Barcelona, Spain. Electronic address:
The utilization of biomimetic membranes supported by advanced self-assembled monolayers is gaining attraction as a promising sensing tool. Biomimetic membranes offer exceptional biocompatibility and adsorption capacity upon degradation, transcending their role as mere research instruments to open new avenues in biosensing. This study focused on anchoring a sparsely tethered bilayer lipid membrane onto a self-assembled monolayer composed of a biodegradable polymer, functionalized with poly(ethylene glycol)-cholesterol moieties, for lipid membrane integration.
View Article and Find Full Text PDFCarrier Protein Interaction with Competing Adenylation and Epimerization Domains in a Nonribosomal Peptide Synthetase Analyzed by FRET.
Angew Chem Int Ed Engl
May 2024
Institute of Biochemistry, Department of Chemistry and Pharmacy, University of Münster, Corrensstraße 36, 48149, Münster, Germany.
In multi-domain nonribosomal peptide synthetases (NRPSs) the order of domains and their catalytic specificities dictate the structure of the peptide product. Peptidyl-carrier proteins (PCPs) bind activated amino acids and channel elongating peptidyl intermediates along the protein template. To this end, fine-tuned interactions with the catalytic domains and large-scale PCP translocations are necessary.
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