Proteolytically stable peptides by incorporation of α-Tfm amino acids

Koksch B, Sewald N, Hofmann H-J, Burger K, Jakubke H-D (1997)
Journal of Peptide Science 3(3): 157-167.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
Koksch, Beate; Sewald, NorbertUniBi ; Hofmann, Hans-Jörg; Burger, Klaus; Jakubke, Hans-Dieter
Einrichtung
Fakultät für Chemie > Organische Chemie III
Erscheinungsjahr
1997
Zeitschriftentitel
Journal of Peptide Science
Band
3
Ausgabe
3
Seite(n)
157-167
ISSN
1075-2617
eISSN
1099-1387
Page URI
https://pub.uni-bielefeld.de/record/1869190

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Koksch B, Sewald N, Hofmann H-J, Burger K, Jakubke H-D. Proteolytically stable peptides by incorporation of α-Tfm amino acids. Journal of Peptide Science. 1997;3(3):157-167.
Koksch, B., Sewald, N., Hofmann, H. - J., Burger, K., & Jakubke, H. - D. (1997). Proteolytically stable peptides by incorporation of α-Tfm amino acids. Journal of Peptide Science, 3(3), 157-167. https://doi.org/10.1002/(SICI)1099-1387(199705)3:3<157::AID-PSC94>3.0.CO;2-W
Koksch, Beate, Sewald, Norbert, Hofmann, Hans-Jörg, Burger, Klaus, and Jakubke, Hans-Dieter. 1997. “Proteolytically stable peptides by incorporation of α-Tfm amino acids”. Journal of Peptide Science 3 (3): 157-167.
Koksch, B., Sewald, N., Hofmann, H. - J., Burger, K., and Jakubke, H. - D. (1997). Proteolytically stable peptides by incorporation of α-Tfm amino acids. Journal of Peptide Science 3, 157-167.
Koksch, B., et al., 1997. Proteolytically stable peptides by incorporation of α-Tfm amino acids. Journal of Peptide Science, 3(3), p 157-167.
B. Koksch, et al., “Proteolytically stable peptides by incorporation of α-Tfm amino acids”, Journal of Peptide Science, vol. 3, 1997, pp. 157-167.
Koksch, B., Sewald, N., Hofmann, H.-J., Burger, K., Jakubke, H.-D.: Proteolytically stable peptides by incorporation of α-Tfm amino acids. Journal of Peptide Science. 3, 157-167 (1997).
Koksch, Beate, Sewald, Norbert, Hofmann, Hans-Jörg, Burger, Klaus, and Jakubke, Hans-Dieter. “Proteolytically stable peptides by incorporation of α-Tfm amino acids”. Journal of Peptide Science 3.3 (1997): 157-167.

16 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Probing the Outstanding Local Hydrophobicity Increases in Peptide Sequences Induced by Incorporation of Trifluoromethylated Amino Acids.
Gadais C, Devillers E, Gasparik V, Chelain E, Pytkowicz J, Brigaud T., Chembiochem 19(10), 2018
PMID: 29513394
Enantioselective synthesis of α-perfluoroalkylated prolines, their 6,7-membered homologues and derivatives.
Voznesenskaia NG, Shmatova OI, Khrustalev VN, Nenajdenko VG., Org Biomol Chem 16(38), 2018
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Position-dependent impact of hexafluoroleucine and trifluoroisoleucine on protease digestion.
Huhmann S, Stegemann AK, Folmert K, Klemczak D, Moschner J, Kube M, Koksch B., Beilstein J Org Chem 13(), 2017
PMID: 29564015
Synthesis of protected enantiopure (R) and (S)-α-trifluoromethylalanine containing dipeptide building blocks ready to use for solid phase peptide synthesis.
Devillers E, Pytkowicz J, Chelain E, Brigaud T., Amino Acids 48(6), 2016
PMID: 26920748
Synthesis of α,ω-polyfluorinated α-amino acid derivatives and δ,δ-difluoronorvaline.
Ulbrich D, Daniliuc CG, Haufe G., Org Biomol Chem 14(9), 2016
PMID: 26857261
(R)-α-trifluoromethylalanine containing short peptide in the inhibition of amyloid peptide fibrillation.
Botz A, Gasparik V, Devillers E, Hoffmann AR, Caillon L, Chelain E, Lequin O, Brigaud T, Khemtemourian L., Biopolymers 104(5), 2015
PMID: 25968595
Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones.
Cho J, Sawaki K, Hanashima S, Yamaguchi Y, Shiro M, Saigo K, Ishida Y., Chem Commun (Camb) 50(69), 2014
PMID: 25025862
Impact of fluorination on proteolytic stability of peptides in human blood plasma.
Asante V, Mortier J, Schlüter H, Koksch B., Bioorg Med Chem 21(12), 2013
PMID: 23623671
Efficient asymmetric synthesis of trifluoromethylated β-aminophosphonates and their incorporation into dipeptides.
Turcheniuk KV, Poliashko KO, Kukhar VP, Rozhenko AB, Soloshonok VA, Sorochinsky AE., Chem Commun (Camb) 48(94), 2012
PMID: 23090101
Enantioselective synthesis of (2R, 3S)- and (2S, 3R)-4,4,4-trifluoro-N-Fmoc-O-tert-butyl-threonine and their racemization-free incorporation into oligopeptides via solid-phase synthesis.
Xiao N, Jiang ZX, Yu YB., Biopolymers 88(6), 2007
PMID: 17702025
Exploration of backbone space in foldamers containing alpha- and beta-amino acid residues: developing protease-resistant oligomers that bind tightly to the BH3-recognition cleft of Bcl-xL.
Sadowsky JD, Murray JK, Tomita Y, Gellman SH., Chembiochem 8(8), 2007
PMID: 17503422
Domino reactions with fluorinated five-membered heterocycles. alpha-Trifluoromethyl alpha-amino acids with unsaturated side-chains.
Burger K, Hennig L, Tsouker P, Spengler J, Albericio F, Koksch B., Amino Acids 31(4), 2006
PMID: 16715414
The introduction of fluorine atoms or trifluoromethyl groups in short cationic peptides enhances their antimicrobial activity.
Giménez D, Andreu C, del Olmo Ml, Varea T, Diaz D, Asensio G., Bioorg Med Chem 14(20), 2006
PMID: 16809042
Methyltrifluoropyruvate imines possessing N-oxalyl and N-phosphonoformyl groups--precursors to a variety of alpha-CF3-alpha-amino acid derivatives.
Skarpos H, Vorob'eva DV, Osipov SN, Odinets IL, Breuer E, Röschenthaler GV., Org Biomol Chem 4(19), 2006
PMID: 16990943
Evaluation of the molecular interactions of fluorinated amino acids with native polypeptides.
Jäckel C, Seufert W, Thust S, Koksch B., Chembiochem 5(5), 2004
PMID: 15122644
Microsomal triglyceride transfer protein inhibitors: discovery and synthesis of alkyl phosphonates as potent MTP inhibitors and cholesterol lowering agents.
Magnin DR, Biller SA, Wetterau J, Robl JA, Dickson JK, Taunk P, Harrity TW, Lawrence RM, Sun CQ, Wang T, Logan J, Fryszman O, Connolly F, Jolibois K, Kunselman L., Bioorg Med Chem Lett 13(7), 2003
PMID: 12657277

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