Synthesis and properties of tuftsin, L-threonyl-L-lysil-L-prolyl-L-arginine

Vičar, Jaroslav; Gut, V.; Frič, I.; Bláha, K.

doi:10.1135/cccc19763467

Cited by 25 publications

(4 citation statements)

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“…112). 3D structures of TF were studied both by physico-chemical measurements [ IR (113), CD (114), NMR (115-117)] and energy calculations (48,116,118,119). At the early stage, two different models for biologically active tuftsin conformations were proposed.…”

Section: Thyrotropin-releasing Horrnone(pglu-his-pro-nfl2 Trh Trf mentioning

confidence: 99%

Computational molecular modeling in peptide drug design

Nikiforovich

1994

International Journal of Peptide and Protein Research

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The review concentrates on practical applications of computer molecular modeling in peptide drug design. The examples of the predictions (successful or not) made by computational modeling before synthesis of peptide analogs, not the explanations provided after synthesis and biological testing of peptides, are discussed. The review spans over 20 years of predictions made by computer molecular modeling for bradykinin, angio‐tensin, thyrotropin‐releasing factor, tuftsin, substance P, CCK‐related peptides, luliberin, α‐melanotropin and opioid peptides. The described examples are discussed in terms of finding the optimal way to use computer modeling for peptide design. The step‐by‐step‘technology’of peptide design is outlined in detail. © Munksgaard 1994.

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Section: Thyrotropin-releasing Horrnone(pglu-his-pro-nfl2 Trh Trf mentioning

confidence: 99%

Computational molecular modeling in peptide drug design

Nikiforovich

1994

International Journal of Peptide and Protein Research

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“…Di-[err.-butyl-dicarbonate (4.6 g, 2 1.1 mmol) and 1 N NaOH (19.2 mL) were added to an ice-cold solution of H-[Glc(Ac)4P]Hyp-OH acetate (10 g, 19.2 mmol) in 30% aqueous dioxane (150 mL). The reaction mixture was stirred 1 h in an ice-bath by keeping the pH to [8][9] with 1 N NaOH. The organic solvent was removed and the aqueous solution was extracted with ethyl acetate (4 x 20 mL), acidified to pH 4.5 with 1 N HCI and reextracted with ethyl acetate (4 x 20 mL).…”

Section: Boc-[glc(ac)4p/hvp-oh (Ivb) Crude Z-[ Glc(ac)4p]mentioning

confidence: 99%

Synthesis and biological activity of [L‐hydroxyproline]³‐tuftsin analogue and its α‐ or β‐O‐D‐glucosylated derivatives

Biondi

Filira

Rocchi

et al. 1993

International Journal of Peptide and Protein Research

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Syntheses are described of the Hyp3‐tuftsin analogue and of its derivatives α‐ or β‐O‐glycosylated at the side chain function of the hydroxyproline residue. The carbohydrate‐free tetrapeptide was prepared by reacting Z‐Thr‐Lys(Z)‐OH with H‐Hyp‐Arg(NO2)‐OBzl by the mixed anhydride procedure. In the synthesis of the α‐glycosylated analogue the O‐glycosyl amino acid was incorporated by reacting Boc‐(Glcα+β)Hyp‐OH with H‐Arg(NO2)‐OBzl through the same procedure. The α‐glucosylated dipeptide was isolated from the diastereomeric mixture, selectively deblocked, and acylated with Z‐Thr‐Lys(Z)‐OH by the mixed anhydride procedure. In the preparation of the β‐glucosylated analogue the BOP procedure was used for reacting Boc‐[Glc(Ac)4β]Hyp‐OH with H‐Arg(NO)2‐OBzl was well as for the final coupling to tetrapeptide. Removal of protecting groups from crude tetrapeptides was achieved by catalytic hydrogenation. Deacetylation of the sugar moiety of the β‐glucosylated tetrapeptide was achieved by treatment with sodium methoxide in methanol. The synthetic compounds were isolated by ion exchange chromatography, and characterized by elemental analysis, amino acid analysis, optical rotation and proton NMR. Their capacity to evoke the release of interleukin 1 from mouse peritoneal macrophages and to modulate immunogenic activity of antigen‐fed cells was evaluated, in comparison with tuftsin and rigin. All of the analogues were found to possess tuftsin‐like activity.

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“…Although only a limited number of relevant reports have been published, it seems that rather conflicting conclusions are drawn. Based on circular dichroism study with tuftsin and tuftsin esterified at the C-terminal, it was suggested by Vicar et al (26), that the peptide may have some pseudo-cyclic structure in which the negative carboxylic group of Arg4 ionically interacts with the positively charged ammonium side chain of Lys2. M.R., and I.…”

Section: On the Structure Of Tuftsinmentioning

confidence: 99%

“…)5) N. D. 24 Thr-Lys-His-Arg 0.150.2(P)(J4.35) N.D. 25 Thr-Lys-Lys-Arg 0.45(p)135) N.D. 26 Thr-Lys-Ser-Arg 00.I(P)() 4.35) N. D. 21 Thr-Lys-Sar-Arg 0.I(P)i35 1 N. D.…”

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Tuftsin, Thr-Lys-Pro-Arg

Fridkin

Gottlieb

1981

Immunologically Active Peptides

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Tuftsin, a natural occurring tetrapeptide, has been found to exhibit several biological activities connected with immune system function. Although little is known about tuftsin's 'biogenesis', much information has been gleaned about its structure-function relationships, which have shown that several features of the molecule are essential for expression offull biological activity. Furthermore, specific receptor sites for tuftsin have been found to exist exclusively on phagocytic cells. Research indicates that tuftsin binding to target cells effect intracellular calcium and cyclic nucleotide levels. Implication of these facts on tuftsin's mode of action are discussed.Basic peptidic segments resembling tuftsin are found in a variety of regulatory peptides. Questions are, therefore, raised as to the biospecificity and cross-reactivity of these sequences. Substance P, one such peptide, which binds with and activates tuftsin receptors, is described.In light of tuftsin's therapeutic potential, assays for its determination have been introduced. When applied to analyze human blood serum of normal as well as of various pathological origins, direct correlation was found between tuftsin levels and susceptibility to bacterial infections. Molecular and Cellular Biochemistry 41,73-97 (1981). 0300 8177/81 0041 0073/$05.00.

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Synthesis and properties of tuftsin, L-threonyl-L-lysil-L-prolyl-L-arginine

Cited by 25 publications

References 0 publications

Computational molecular modeling in peptide drug design

Computational molecular modeling in peptide drug design

Synthesis and biological activity of [L‐hydroxyproline]³‐tuftsin analogue and its α‐ or β‐O‐D‐glucosylated derivatives

Tuftsin, Thr-Lys-Pro-Arg

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Synthesis and properties of tuftsin, L-threonyl-L-lysil-L-prolyl-L-arginine

Cited by 25 publications

References 0 publications

Computational molecular modeling in peptide drug design

Computational molecular modeling in peptide drug design

Synthesis and biological activity of [L‐hydroxyproline]3‐tuftsin analogue and its α‐ or β‐O‐D‐glucosylated derivatives

Tuftsin, Thr-Lys-Pro-Arg

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Synthesis and biological activity of [L‐hydroxyproline]³‐tuftsin analogue and its α‐ or β‐O‐D‐glucosylated derivatives