[ad_1]
Avci, F. G., Akbulut, B. S. & Ozkirimli, E. Membrane lively peptides and their biophysical characterization. Biomolecules 8, 1–43 (2018).
Sani, M. A. & Separovic, F. How membrane-active peptides get into lipid membranes. Acc. Chem. Res. 49, 1130–1138 (2016).
Gräslund, A., Madani, F., Lindberg, S., Langel, Ü. & Futaki, S. Mechanisms of mobile uptake of cell-penetrating peptides. J. Biophys. 2011, 414729 (2011).
Heitz, F., Morris, M. C. & Divita, G. Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics. Br. J. Pharmacol. 157, 195–206 (2009).
Lee, H. M. et al. Identification of environment friendly prokaryotic cell-penetrating peptides with purposes in bacterial biotechnology. Commun. Biol. 4, 1–13 (2021).
Munyendo, W. L. L., Lv, H., Benza-Ingoula, H., Baraza, L. D. & Zhou, J. Cell penetrating peptides within the supply of biopharmaceuticals. Biomolecules 2, 187–202 (2012).
Yousef, M. et al. Cell-penetrating dabcyl-containing tetraarginines with spine aromatics as uptake enhancers. Pharmaceutics 15, 141 (2022).
Lee, H. et al. Conjugation of cell-penetrating peptides to antimicrobial peptides enhances antibacterial exercise. ACS Omega 4, 15694–15701 (2019).
Nam, S. H., Park, J. & Koo, H. Latest advances in selective and focused drug/gene supply programs utilizing cell-penetrating peptides. Arch. Pharm. Res. 46, 18–34 (2023).
Eiríksdóttir, E., Konate, Okay., Langel, Ü., Divita, G. & Deshayes, S. Secondary construction of cell-penetrating peptides controls membrane interplay and insertion. Biochim. Biophys. Acta Biomembr. 1798, 1119–1128 (2010).
Gautam, A. et al. CPPsite: A curated database of cell penetrating peptides. Database 2012, 1–7 (2012).
Oikawa, Okay., Islam, M. M., Horii, Y., Yoshizumi, T. & Numata, Okay. Screening of a cell-penetrating peptide library in Escherichia coli: Relationship between cell penetration effectivity and cytotoxicity. ACS Omega 3, 16489–16499 (2018).
Xie, J. et al. Cell-penetrating peptides in analysis and remedy of human illnesses: From preclinical analysis to scientific software. Entrance. Pharmacol. 11, 1–23 (2020).
Di Pisa, M., Chassaing, G. & Swiecicki, J. M. Translocation mechanism(s) of cell-penetrating peptides: Biophysical research utilizing synthetic membrane bilayers. Biochemistry 54, 194–207 (2015).
Derakhshankhah, H. & Jafari, S. Cell penetrating peptides: A concise evaluate with emphasis on biomedical purposes. Biomed. Pharmacother. 108, 1090–1096 (2018).
Desale, Okay., Kuche, Okay. & Jain, S. Cell-penetrating peptides (CPPs): An outline of purposes for bettering the potential of nanotherapeutics. Biomater. Sci. 9, 1153–1188 (2021).
Gori, A. A., Lodigiani, G., Colombarolli, S. G., Bergamaschi, G. & Vitali, A. Cell penetrating peptides: Classification, mechanisms, strategies of examine and purposes. Chem. Med. Chem. 1, e202300236 (2023).
Vaara, M. & Porro, M. Group of peptides that act synergistically with hydrophobic antibiotics in opposition to gram-negative enteric micro organism. Antimicrob. Brokers Chemother. 40, 1801–1805 (1996).
Wojciechowska, M., Miszkiewicz, J. & Trylska, J. Conformational modifications of anoplin, W-MreB1–9, and (KFF)3Okay peptides close to the membranes. Int. J. Mol. Sci. 21, 9672 (2020).
Bai, H. et al. Focusing on RNA polymerase major σ70 as a therapeutic technique in opposition to methicillin-resistant Staphylococcus aureus by antisense peptide nucleic acid. PLoS ONE 7, 1–10 (2012).
Kulik, M. et al. Helix 69 of Escherichia coli 23S ribosomal RNA as a peptide nucleic acid goal. Biochimie 138, 32–42 (2017).
Castillo, J. I., Równicki, M., Wojciechowska, M. & Trylska, J. Antimicrobial synergy between mRNA focused peptide nucleic acid and antibiotics in E. coli. Bioorg. Med. Chem. Lett. 28, 3094–3098 (2018).
Równicki, M. et al. Vitamin B12 as a service of peptide nucleic acid (PNA) into bacterial cells. Sci. Rep. 7, 1–11 (2017).
Wojciechowska, M., Równicki, M., Mieczkowski, A., Miszkiewicz, J. & Trylska, J. Antibacterial peptide nucleic acids: info and views. Int. J. Mol. Sci. 25, 59 (2020).
Hatamoto, M., Nakai, Okay., Ohashi, A. & Imachi, H. Sequence-specific bacterial development inhibition by peptide nucleic acid focused to the mRNA binding web site of 16S rRNA. Appl. Microbiol. Biotechnol. 84, 1161–1168 (2009).
Yavari, N., Goltermann, L. & Nielsen, P. E. Uptake, Stability, and exercise of antisense anti- acpP PNA-peptide conjugates in Escherichia coli and the position of SbmA. ACS Chem. Biol. 16, 471–479 (2021).
Szabó, I. et al. Redesigning of cell-penetrating peptides to enhance their efficacy as a drug supply system. Pharmaceutics 14, 907 (2022).
Melikov, Okay. & Chernomordik, L. V. Arginine-rich cell penetrating peptides: From endosomal uptake to nuclear supply. Cell. Mol. Life Sci. 62, 2739–2749 (2005).
Nan, Y. H., Park, I. S., Hahm, Okay. S. & Shin, S. Y. Antimicrobial exercise, bactericidal mechanism and LPS-neutralizing exercise of the cell-penetrating peptide pVEC and its analogs. J. Pept. Sci. 17, 812–817 (2011).
Faust, J. E., Yang, P. Y. & Huang, H. W. Motion of antimicrobial peptides on bacterial and lipid membranes: A direct comparability. Biophys. J. 112, 1663–1672 (2017).
Budagavi, D. P. & Chugh, A. Antibacterial properties of Latarcin 1 derived cell-penetrating peptides. Eur. J. Pharm. Sci. 115, 43–49 (2018).
Zhu, W. L. et al. Design and mechanism of motion of a novel bacteria-selective antimicrobial peptide from the cell-penetrating peptide Pep-1. Biochem. Biophys. Res. Commun. 349, 769–774 (2006).
Zhu, W. L., Hahm, Okay. S. & Shina, S. Y. Cell selectivity and mechanism of motion of quick antimicrobial peptides designed from the cell-penetrating peptide Pep-1. J. Pept. Sci. 15, 569–575 (2009).
Shai, Y. Mode of motion of membrane lively antimicrobial peptides. Pept. Sci. 66, 236–248 (2002).
Mourtada, R. et al. Design of stapled antimicrobial peptides that overcome antibiotic resistance and in vivo toxicity. Nat Biotechnol. 37, 1186–1197 (2019).
Kim, H. Y., Yum, S. Y., Jang, G. & Ahn, D. R. Discovery of a non-cationic cell penetrating peptide derived from membrane-interacting human proteins and its potential as a protein supply service. Sci. Rep. 5, 1–15 (2015).
Hong, S. Y., Oh, J. E. & Lee, Okay.-H. Impact of D-amino acid substitution on the soundness, the secondary construction, and the exercise of membrane-active peptide. Biochem. Pharmacol. 58, 1775–1780 (1999).
Migoń, D., Neubauer, D. & Kamysz, W. Hydrocarbon stapled antimicrobial peptides. Protein J. 37, 2–12 (2018).
Chapuis, H. et al. Impact of hydrocarbon stapling on the properties of α-helical antimicrobial peptides remoted from the venom of hymenoptera. Amino Acids 43, 2047–2058 (2012).
Blackwell, H. E. & Grubbs, R. H. Extremely environment friendly synthesis of covalently cross-linked peptide helices by ring-closing metathesis. Angew. Chem. Int. Ed. 37, 3281–3284 (1998).
Lau, Y. H., De Andrade, P., Wu, Y. & Spring, D. R. Peptide stapling strategies primarily based on totally different macrocyclisation chemistries. Chem. Soc. Rev. 44, 91–102 (2015).
You, Y. H., Liu, H. Y., Zhu, Y. Z. & Zheng, H. Rational design of stapled antimicrobial peptides. Amino Acids 55, 421–442 (2023).
Walensky, L. D. & Hen, G. H. Hydrocarbon-stapled peptides: Rules, observe, and progress. J. Med. Chem. 57, 6275–6288 (2014).
Hen, G. H., Christian Crannell, W. & Walensky, L. D. Chemical synthesis of hydrocarbon-stapled peptides for protein interplay analysis and therapeutic concentrating on. Curr. Protoc. Chem. Biol. 3, 99–117 (2011).
Luong, H. X., Kim, D.-H., Lee, B.-J. & Kim, Y.-W. Antimicrobial exercise and stability of stapled helices of polybia-MP1. Arch. Pharm. Res. 40, 1414–1419 (2017).
Mourtada, R. et al. Design of stapled antimicrobial peptides which can be steady, unhazardous and kill antibiotic-resistant micro organism in mice. Nat. Biotechnol. 37, 1186–1197 (2019).
Wojciechowska, M., Macyszyn, J., Miszkiewicz, J., Grzela, R. & Trylska, J. Stapled anoplin as an antibacterial agent. Entrance. Microbiol. 12, 772038 (2021).
Stawikowski, G. B. F. M. Introduction to peptide synthesis. Curr. Protoc. Protein Sci. 26, 1–17 (2002).
Kaiser, E., Colescott, R. L., Bossinger, C. D. & Prepare dinner, P. I. Coloration check for detection of free terminal amino teams within the solid-phase synthesis of peptides. Anal. Biochem. 34, 595–598 (1970).
Miles, A. J., Ramalli, S. G. & Wallace, B. A. DichroWeb, a web site for calculating protein secondary construction from round dichroism spectroscopic information. Protein Sci. 31, 37–46 (2022).
Whitmore, L. & Wallace, B. A. Protein secondary construction analyses from round dichroism spectroscopy: Strategies and reference databases. Biopolymers 89, 392–400 (2008).
Abdul-Gader, A., Miles, A. J. & Wallace, B. A. A reference dataset for the analyses of membrane protein secondary constructions and transmembrane residues utilizing round dichroism spectroscopy. Bioinformatics 27, 1630–1636 (2011).
Case, D. A. et al. Amber 2020 (College of California, 2020).
Khoury, G. A. et al. Forcefield-NCAA: Ab initio cost parameters to assist within the discovery and design of therapeutic proteins and peptides with unnatural amino acids and their software to enhance inhibitors of the compstatin household. ACS Synth. Biol. 3, 855–869 (2014).
Cheng, X., Jo, S., Lee, H. S., Klauda, J. B. & Im, W. CHARMM-GUI micelle builder for pure/combined micelle and protein/micelle advanced programs. J. Chem. Inf. Mannequin. 53, 2171–2180 (2013).
Allouche, A. Software program information and updates gabedit: A graphical consumer interface for computational chemistry softwares. J. Comput. Chem. 32, 174–182 (2012).
Turro, N. J. & Yekta, A. Luminescent probes for detergent options: A easy process for willpower of the imply aggregation variety of micelles. J. Am. Chem. Soc 100, 5951–5952 (1978).
Croonen, Y. et al. Affect of salt, detergent focus, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecyl sulfate with m-dicyanobenzene. J. Phys. Chem. 87, 1426–1431 (1983).
Bales, B. L., Messina, L., Vidal, A., Peric, M. & Nascimento, O. R. Precision relative aggregation quantity determinations of SDS micelles utilizing a spin probe. A mannequin of micelle floor hydration. J. Phys. Chem. B 102, 10347–10358 (1998).
Palazzesi, F., Calvaresi, M. & Zerbetto, F. A molecular dynamics investigation of construction and dynamics of SDS and SDBS micelles. Tender Matter 7, 9148–9156 (2011).
Maier, J. A. et al. ff14SB: Bettering the accuracy of protein facet chain and spine parameters from ff99SB. J. Chem. Idea Comput. 11, 3696–3713 (2015).
Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W. & Klein, M. L. Comparability of easy potential features for simulating liquid water. J. Chem. Phys. 79, 926–935 (1983).
Joung, I. S. & Cheatham, T. E. Dedication of alkali and halide monovalent ion parameters to be used in explicitly solvated biomolecular simulations. J. Phys. Chem. B 112, 9020–9041 (2008).
Homeyer, N., Horn, A. H. C., Lanig, H. & Sticht, H. AMBER force-field parameters for phosphorylated amino acids in several protonation states: Phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine. J. Mol. Mannequin. 12, 281–289 (2006).
Vanommeslaeghe, Okay. et al. CHARMM basic pressure area: A pressure area for drug-like molecules suitable with the CHARMM all-atom additive organic pressure fields. J. Comput. Chem. 31, 671–690 (2010).
Hopkins, C. W., Le Grand, S., Walker, R. C. & Roitberg, A. E. Lengthy-time-step molecular dynamics by means of hydrogen mass repartitioning. J. Chem. Idea Comput. 11, 1864–1874 (2015).
Kabsch, C. S. W. Dictionary of protein secondary construction: Sample recognition of hydrogen-bonded and geometrical options. Sing. Med. J. 12, 2577–2637 (1983).
Roe, D. R. & Cheatham, T. E. PTRAJ and CPPTRAJ: Software program for processing and evaluation of molecular dynamics trajectory information. J. Chem. Idea Comput. 9, 3084–3095 (2013).
Hunter, J. D. Matplotlib: A 2D graphics setting. Comput. Sci. Eng. 9, 90–95 (2007).
Humphrey, W., Dalke, A. & Schulten, Okay. VMD: Visible molecular dynamics. J. Mol. Graph. 7855, 33–38 (1996).
Zhong, C. et al. Antimicrobial peptides conjugated with fatty acids on the facet chain of D-amino acid guarantees antimicrobial efficiency in opposition to multidrug-resistant micro organism. Eur. J. Pharm. Sci. 141, 105123 (2020).
Merkler, D. J. C-terminal amidated peptides: Manufacturing by the in vitro enzymic amidation of glycine-extended peptides and the significance of the amide to bioactivity. Chem. Inform. 25, 450–456 (2010).
Toniolo, C., Polese, A., Formaggio, F., Crisma, M. & Kamphuis, J. Round dichroism spectrum of a peptide 310-helix. J. Am. Chem. Soc. 118, 2744–2745 (1996).
Watson, R. M. et al. Conformational modifications in pediocin AcH upon vesicle binding and approximation of the membrane-bound construction in detergent micelles. Biochemistry 40, 14037–14046 (2001).
Dorovkov, M. V., Kostyukova, A. S. & Ryazanov, A. G. Phosphorylation of annexin A1 by TRPM7 kinase: A change regulating the induction of an α-helix. Biochemistry 50, 2187–2193 (2011).
Doig, A. J., Macarthur, M. W., Stapley, B. J. & Thornton, J. M. Constructions of N-termini of helices in proteins. Protein Sci. 6, 147–155 (1997).
Czapinska, H. & Otlewski, J. Structural and energetic determinants of the S1-site specificity in serine proteases. Eur. J. Biochem. 260, 571–595 (1999).
Schafmeister, C. E., Po, J. & Verdine, G. L. An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides. J. Am. Chem. Soc. 122, 5891–5892 (2000).
Malanovic, N. & Lohner, Okay. Gram-positive bacterial cell envelopes: The impression on the exercise of antimicrobial peptides. Biochim. Biophys. Acta Biomembr. 1858, 936–946 (2016).
Łoś, J. M., Łoś, M., Wȩgrzyn, A. & Wȩgrzyn, G. Hydrogen peroxide-mediated induction of the Shiga toxin-converting lambdoid prophage ST2-8624 in Escherichia coli O157:H7. FEMS Immunol. Med. Microbiol. 58, 322–329 (2010).
Hrabák, J. et al. Worldwide clones of Klebsiella pneumoniae and Escherichia coli with extended-spectrum β-lactamases in a Czech Hospital. J. Clin. Microbiol. 47, 3353–3357 (2009).
29213 @ www.atcc.org. https://www.atcc.org/merchandise/29213.
baa-1720 @ www.atcc.org. https://www.atcc.org/merchandise/baa-1720.
27853 @ www.atcc.org. https://www.atcc.org/merchandise/27853.
Schoch, C. L. et al. NCBI taxonomy: A complete replace on curation, assets and instruments. Database 2020, 1–21 (2020).
Li, B. et al. Colistin resistance gene mcr-1 mediates cell permeability and resistance to hydrophobic antibiotics. Entrance. Microbiol. 10, 1–7 (2020).
Krishnamurthy, M. et al. Enhancing the antibacterial exercise of polymyxins utilizing a nonantibiotic drug. Infect. Drug Resist. 12, 1393–1405 (2019).
Olaitan, A. O., Morand, S. & Rolain, J. M. Mechanisms of polymyxin resistance: Acquired and intrinsic resistance in micro organism. Entrance. Microbiol. 5, 1–18 (2014).
Henriques, S. T., Melo, M. N. & Castanho, M. A. R. B. Cell-penetrating peptides and antimicrobial peptides: How totally different are they?. Biochem. J. 399, 1–7 (2006).
Bahnsen, J. S., Franzyk, H., Sandberg-Schaal, A. & Nielsen, H. M. Antimicrobial and cell-penetrating properties of penetratin analogs: Impact of sequence and secondary construction. Biochim. Biophys. Acta Biomembr. 1828, 223–232 (2013).
Splith, Okay. & Neundorf, I. Antimicrobial peptides with cell-penetrating peptide properties and vice versa. Eur. Biophys. J. 40, 387–397 (2011).
[ad_2]