Academic literature on the topic 'Poly-α-amino acids'

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Journal articles on the topic "Poly-α-amino acids"

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Kino, Kuniki, Toshinobu Arai та Yasuhiro Arimura. "Poly-α-Glutamic Acid Synthesis Using a Novel Catalytic Activity of RimK fromEscherichia coliK-12". Applied and Environmental Microbiology 77, № 6 (2011): 2019–25. http://dx.doi.org/10.1128/aem.02043-10.

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ABSTRACTPoly-l-α-amino acids have various applications because of their biodegradable properties and biocompatibility. Microorganisms contain several enzymes that catalyze the polymerization ofl-amino acids in an ATP-dependent manner, but the products from these reactions contain amide linkages at the side residues of amino acids: e.g., poly-γ-glutamic acid, poly-ε-lysine, and cyanophycin. In this study, we found a novel catalytic activity of RimK, a ribosomal protein S6-modifying enzyme derived fromEscherichia coliK-12. This enzyme catalyzed poly-α-glutamic acid synthesis from unprotectedl-gl
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Cohen-Arazi, Naomi, Abraham J. Domb та Joshua Katzhendler. "Poly(α -hydroxy alkanoic acid)s Derived From α -Amino Acids". Macromolecular Bioscience 13, № 12 (2013): 1689–99. http://dx.doi.org/10.1002/mabi.201300266.

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Sedlačík, Tomáš, Vladimír Proks, Miroslav Šlouf, Miroslava Dušková-Smrčková, Hana Studenovská та František Rypáček. "Macroporous Biodegradable Cryogels of Synthetic Poly(α-amino acids)". Biomacromolecules 16, № 11 (2015): 3455–65. http://dx.doi.org/10.1021/acs.biomac.5b01224.

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Sedlačík, T., O. K. Acar, H. Studenovská та ін. "Chondrogenic potential of macroporous biodegradable cryogels based on synthetic poly(α-amino acids)". Soft Matter 14, № 2 (2018): 228–38. http://dx.doi.org/10.1039/c7sm02074k.

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Masař, Bohumil, Pavel Schmidt, Hana Pivcová та Pavel Čefelín. "α-Aminoacyl derivatives of α,ω-diaminopoly(oxyethylene)". Collection of Czechoslovak Chemical Communications 52, № 8 (1987): 1922–27. http://dx.doi.org/10.1135/cccc19871922.

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By reacting p-nitrophenyl esters of L-α-amino acids with α-(3-aminopropyl)-ω-(aminomethyl)-poly(oxyethylene), diamides having the structure [X-NHCH(R)CONH]2Mx' were prepared, X being the protective group Boc or Z, R being residues of glutamic and aspartic acid, phenylalanine and tyrosine, and Mx' being the poly(oxyethylene) chain with the (-CH2)3- and -CH2- endgroups. The diamides were characterized by IR and 1H NMR spectroscopy and thin-layer chromatography. After complete removal of tert-butyloxycarbonyl groups from diamides (X = Boc), deprotected α-aminoacyl derivatives were characterized a
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Guo, Yifei, Yiping Shen, Bo Yu, et al. "Hydrophilic Poly(glutamic acid)-Based Nanodrug Delivery System: Structural Influence and Antitumor Efficacy." Polymers 14, no. 11 (2022): 2242. http://dx.doi.org/10.3390/polym14112242.

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Poly(amino acids) have advanced characteristics, including unique secondary structure, enzyme degradability, good biocompatibility, and stimuli responsibility, and are suitable as drug delivery nanocarriers for tumor therapy. The isoform structure of poly(amino acids) plays an important role in their antitumor efficacy and should be researched in detail. In this study, two kinds of pH-sensitive isoforms, including α-poly(glutamic acid) (α-PGA) and γ-PGA, were selected and used as nanocarriers to prepare a nanodrug delivery system. According to the preparation results, α-PGA can be used as an i
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Votavová, Hana, Ferenc Hudecz, Judit Kajtár, Jaroslav Šponar, Karel Bláha, and Mária Szekerke. "Conformation of branched polypeptides based on poly(L-lysine): The effect of terminal amino acids in the branches." Collection of Czechoslovak Chemical Communications 50, no. 1 (1985): 228–44. http://dx.doi.org/10.1135/cccc19850228.

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CD Spectra of branched polypeptides based on poly(L-lysine) and containing three DL-alanine residues and one to three other L- or D-amino acid residues in the branches were measured in water, water-methanol and water-trifluoroethanol mixtures. In aqueous solutions dependence of the CD spectra on pH and ionic strength was studied. The effect of branch elongation was followed mainly with compounds containing glutamic acid. One terminal D-amino acid residue and also an extension by two L- or D-amino acid residues does not hinder the α-helix formation in the backbone but affects the conditions of
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Tolmachev, Dmitry, Natalia Lukasheva, George Mamistvalov, and Mikko Karttunen. "Influence of Calcium Binding on Conformations and Motions of Anionic Polyamino Acids. Effect of Side Chain Length." Polymers 12, no. 6 (2020): 1279. http://dx.doi.org/10.3390/polym12061279.

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Investigation of the effect of CaCl2 salt on conformations of two anionic poly(amino acids) with different side chain lengths, poly-(α-l glutamic acid) (PGA) and poly-(α-l aspartic acid) (PASA), was performed by atomistic molecular dynamics (MD) simulations. The simulations were performed using both unbiased MD and the Hamiltonian replica exchange (HRE) method. The results show that at low CaCl2 concentration adsorption of Ca2+ ions lead to a significant chain size reduction for both PGA and PASA. With the increase in concentration, the chains sizes partially recover due to electrostatic repul
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Zavradashvili, Nino, Jordi Puiggali та Ramaz Katsarava. "Artificial Polymers made of α-amino Acids - Poly(Amino Acid)s, Pseudo-Poly(Amino Acid)s, Poly(Depsipeptide)s, and Pseudo-Proteins". Current Pharmaceutical Design 26, № 5 (2020): 566–93. http://dx.doi.org/10.2174/1381612826666200203122110.

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Degradable polymers (DPs) - “green materials” of the future, have an innumerable use in biomedicine, particularly in the fields of tissue engineering and drug delivery. Among these kind of materials naturally occurring polymers - proteins which constituted one of the most important “bricks of life” - α-amino acids (AAs) are highly suitable. A wide biomedical applicability of proteins is due to special properties such as a high affinity with tissues and releasing AAs upon biodegradation that means a nutritive potential for cells. Along with these positive characteristics proteins as biomedical
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Ebert, G., та H. Lukasch. "Trifluoromethanesulphonic acid as an α-helix promoting agent for basic poly(α-amino acids)". International Journal of Biological Macromolecules 8, № 3 (1986): 142–44. http://dx.doi.org/10.1016/0141-8130(86)90015-2.

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Dissertations / Theses on the topic "Poly-α-amino acids"

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Hernik-Magoń, Agnieszka. "Amyloidogenne właściwości peptydów (L-Glu)n." Doctoral thesis, 2018. https://depotuw.ceon.pl/handle/item/3062.

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Częściowa destabilizacja struktury natywnej białka, może faworyzować zachodzenie procesu agregacji, co wiąże się z powstawaniem wysoce uporządkowanych (β-kartkowych), fibrylarnych struktur, które noszą nazwę amyloidów. Odkładanie się takich nierozpuszczalnych struktur w tkankach jest często powiązane z etiologią szeregu chorób degeneracyjnych m.in. chorobami Alzheimera, Parkinsona, czy Huntingtona. Postulat, że formowanie fibryli amyloidowych jest generyczną cechą białek jako poliamidów poszerzył grupę badanych w tym kontekście białek o syntetyczne peptydy, w tym poli-α-aminokwasy. Uproszczeni
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Book chapters on the topic "Poly-α-amino acids"

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Kohn, Joachim, and Robert Langer. "Backbone modification of synthetic poly-α-L-amino acids." In Peptides. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_198.

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Li, Xiaoling, David B. Bennett, Nathan W. Adams, and Sung Wan Kim. "Poly(α-amino acid)—Drug Conjugates." In ACS Symposium Series. American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0469.ch011.

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Hayashi, Toshio. "Poly(α-Amino Acids): Biodegradation, Medical Applications." In Encyclopedia of Biomedical Polymers and Polymeric Biomaterials. Taylor & Francis, 2015. http://dx.doi.org/10.1081/e-ebpp-120051911.

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Gold, Douglas G., Wilmer G. Miller, Taner Z. Sen, and Andrzej Kloczkowski. "Poly(L-alanine)." In Polymer Data Handbook. Oxford University PressNew York, NY, 2009. http://dx.doi.org/10.1093/oso/9780195181012.003.0055.

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Abstract Major Applications Serves as a model for various proteins. Properties of Special Interest Two crystalline forms of poly(l-alanine), the α-helix and β-sheet, have been observed. Synthesis Similar to the synthesis of poly(γ -benzyl-l-glutamate) (see the entry on Poly(γ -benzyl-l-glutamate) in this handbook); involves the conversion of the amino acid to the N-carboxyanhydride (NCA) monomer by reaction with phosgene gas followed by polymerization of the NCA with an appropriate initiator (e.g., n-butyl amine). Typical comonomers include other amino acid NCAs.
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