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'Peptide synthesis' in keywords

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1	Author	K. Eisele	Requires cookie*
	Title	Sequence Variation on an Antibiotically Active Tripeptide Seven tripeptides with the sequence L-Arg-D,L-X-L-Phe were synthesised. Three of these peptides showed anti- biotical activity on fungi. The amino-and the carboxylic terminus of the peptide L-Arg-D,L-Phe-L-Phe, which showed antibiotical activity, were changed to give the sequences L-X-D,L-Phe-L-Phe or L-Arg-D,L-Phe-L-X respectively
	Abstract	The resulting tripeptides showed no antibiotical activity.
	Reference	(Z. Naturforsch. 30c, 541 [1975]; eingegangen am 11. Februar/3. April 1975)
	Published	1975
	Keywords	Antibiotics, Sequence Variation, Peptide Synthesis
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	TEI-XML for	default:Reihe_C/30/ZNC-1975-30c-0541_n.pdf
	Identifier	ZNC-1975-30c-0541_n
	Volume	30

2	Author		Requires cookie*
	Title	Synthese eines Peptids m it vermutlicher W irkung des W achstum shorm on-freisetzenden Hormons (G H -R H ) A new synthesis for the tripeptide Pyr- Ser-Gly-NH2, with mutual GH-RH activity is described. Z-L-Pyr-OH is reacted with HO- NSu to the protected amino acid derivative Z-L-Pyr-ONSu. Further intermediates in the synthesis are Z-L-Pyr-L-Ser(Bzl)-OH and Z-L-Pyr-L-Ser(Bzl)-Gly-NHa
	Abstract	Synthesis of a P eptide w ith Suggested A ctivity of G row th H orm one-R eleasing H orm one (GH-RH) K a r l Z e c h u n d W o l f g a n g V o e l t e r Peptide
	Reference	(Z. Naturforsch. 29b, 818—819 [1974]; eingegangen am 9. Oktober 1974)
	Published	1974
	Keywords	hormones, Hypothalamus-releasing hormones, Peptide synthesis
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	TEI-XML for	default:Reihe_B/29/ZNB-1974-29b-0818_n.pdf
	Identifier	ZNB-1974-29b-0818_n
	Volume	29

3	Author	Hubert Kalbacher, Claus Bürvenich, Stefan Fuchs, Hans Horn, Wolfgang Klingler, Emanuel Pietrzik, Karl Zech, Wolfgang Voelter	Requires cookie*
	Title	Totalsynthese von Somatostatin, I Total Synthesis of Somatostatin, I
	Abstract	Experimental details of the syntheses of five peptide fragments, used for the total synthesis of somatostatin, are described. N-Hydroxysuccinimide esters and DCC are used for forming the peptide bonds. The amino acid side chains are protected by trityl, tert-butyloxycarbonyl and benzyl groups.
	Reference	(Z. Naturforsch. 31b, 1702—1707 [1976]; eingegangen am 28. September 1976)
	Published	1976
	Keywords	Peptide Synthesis, Peptide Hormones, Hypothalamus-releasing Hormones, Somatostatin
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	TEI-XML for	default:Reihe_B/31/ZNB-1976-31b-1702.pdf
	Identifier	ZNB-1976-31b-1702
	Volume	31

4	Author	Anders Ljungqvist, Karl Folkers	Requires cookie*
	Title	Study of Hydrogenolytic Cleavage of Peptide-Resin Benzyl Ester Bonds for Synthesis of Protected Fragments of the Human Leukocyte Interferon
	Abstract	Three Boc-protected fragments of the human leukocyte interferon, LeIFA, have been synthesized: I, BOC LeIFA (99-105) (BOC-Val-Ile-Gln-Gly-Val-Gly-Val); II, BOC LeIFA (116-119) (BOC-Ile-Leu-Ala-Val); III, BOC LeIFA (123-126) (BOC-Phe-Gln-Arg(Tos)-Ile). The presence of the Boc-group was desired so that these peptides could serve as intermediates in fragment condensation toward larger segments of interferon. To achieve these intermediates, a study was desirable on three methods of cleavage of the benzyl ester-polymer bonds. It was found that hydrogenolysis with hydrogen and palla-dium generated in situ was distinctly superior to transfer hydrogenation with ammonium formate or cyclohexene. An effective swelling of the peptide-resin to allow penetration of palladium acetate into the matrix and mobility of the peptide chains on the resin to expose the benzyl ester bond to hydrogenolysis appear to be essential conditions for the best cleavage.
	Reference	Z. Naturforsch. 38b, 1022—1024 (1983); received May 2 1983
	Published	1983
	Keywords	Interferon, Peptide Synthesis, Hydrogenation, Palladium Black, Conformation
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	TEI-XML for	default:Reihe_B/38/ZNB-1983-38b-1022.pdf
	Identifier	ZNB-1983-38b-1022
	Volume	38

5	Author	Eugen Schaich, Friedhelm Schneider	Requires cookie*
	Title	Synthese einer Partialsequenz aus dem aktiven Zentrum der Streptokokken-Protease Synthesis of a Fragment of the Active Center of the Streptococcal Proteinase, IV
	Abstract	The synthesis of the protected peptide Boc-His-Cys (M Bzl)-Val-Ala-Thr-Ala-NoHs (OH) is de scribed. This peptide is a fragment of an active center sequence of the streptococcal proteinase (EC 3.4.22.10) containing the essential SH-group of the enzyme.
	Reference	(Z. Naturforsch. 29c, 457 [1974]; eingegangen am 22. März 1974)
	Published	1974
	Keywords	Streptococcal-Proteinase, Active Center-Peptide, Peptide Synthesis
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	TEI-XML for	default:Reihe_C/29/ZNC-1974-29c-0457.pdf
	Identifier	ZNC-1974-29c-0457
	Volume	29

6	Author	Eugen Schaich, Friedhelm Schneider	Requires cookie*
	Title	Synthese einer Partialsequenz aus dem aktiven Zentrum der Streptokokken-Protease Synthesis of a Fragment of the Active Center of the Streptococcal Proteinase, V
	Abstract	The synthesis of the protected peptides Boc-Val-Ala-Thr-Ala-Thr-Ala-Gln-Ile-OH and Thr-Ala-Gln-Ile-Met-Lys(Z)-NH2 is described. These sequences are fragments of an active center peptide of the streptococcal proteinase (EC 3.4.22.10).
	Reference	(Z. Naturforsch. 29c, 464 [1974]; eingegangen am 22. März 1974)
	Published	1974
	Keywords	Streptococcal-Proteinase, Active Center-Peptide, Peptide Synthesis
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	TEI-XML for	default:Reihe_C/29/ZNC-1974-29c-0464.pdf
	Identifier	ZNC-1974-29c-0464
	Volume	29

7	Author	Andreas Raschig, Friedhelm Schneider	Requires cookie*
	Title	Synthese einer Partialsequenz aus dem aktiven Zentrum der Streptokokken-Proteinase The synthesis of the protected peptides Boc-Ala-Ala-Thr-Gly-ONp, Boc-Ala-Thr-Ala-Thr-Ala-ONB and Boc-Ala-Ala-Thr-Gly-His-Cys(X)-Val-Ala-Thr-Ala-Thr
	Abstract	Ala-ONB [X = p-methoxybenzyl, tert-butylmercapto, tetrahydropyranyl-(2)] is described. These peptides are fragments of an active center sequence of the streptococcal proteinase (EC 3.4.22.10) which contains the essential SH group of the enzyme.
	Reference	(Z. Naturforsch. 30c, 745—751 [1975]; eingegangen am 19. August 1975)
	Published	1975
	Keywords	Streptococcal Proteinase, Active Center Peptide, Peptide Synthesis
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	TEI-XML for	default:Reihe_C/30/ZNC-1975-30c-0745.pdf
	Identifier	ZNC-1975-30c-0745
	Volume	30

8	Author	Anders Ljungqvist, Karl Folkers+	Requires cookie*
	Title	Synthesis of a Combined Fragment of Interferon, AeHuIFN a A(30-43)-(123-137)-NH2 Interferon May not be a Sychnologieal Peptide * AeHuIFN a A( 30-43)-( 123-137)-NH2, Ac-Leu-Lys-Asp-Arg-His-Asp-Phe-Gly-Phe- Pro-Gln-Glu-Glu-Phe-Phe-Gln-Arg-Ile-Thr-Leu-Tyr-Leu-Lys-Glu-Lys-Lys-Tyr-Ser- Pro-NH2 was
	Abstract	synthesized toward encompassing the "active site" of the interferons. The design of this 29-amino acid peptide was based on considerations of homology between the different interferons and on combining two regions of interferons, and on known and predicted structural features. The peptide was characterized by amino acid analysis, thin layer chromatography in several systems, and by HPLC. As tested, the peptide neither showed antiviral activity nor blocked antiviral activity of interferon, indicating that the active site was not encompassed or that interferon may not be a sychnologieal peptide.
	Reference	Z. Naturforsch. 38b, 1249—1252 (1983); received June 24 1983
	Published	1983
	Keywords	Interferon, Peptide Synthesis, Antiviral Activity, Synthetic Fragment, Active Site
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	TEI-XML for	default:Reihe_B/38/ZNB-1983-38b-1249.pdf
	Identifier	ZNB-1983-38b-1249
	Volume	38

9	Author	B. Ernd, H. Enkel, L.Ianshan Zhang, C. Arsten, G. Oldam, M. Er, E.Rnst Bayer	Requires cookie*
	Title	Combined Solid Phase and Solution Synthesis of the Fully Protected Segment 74-99 of HIV 1-Protease with the Application of a New Trityl-Linker
	Abstract	A new trityl-linker for the strategy of combined solid phase and solution synthesis has been used for the synthesis of the fully protected segment 74-99 of HIV 1-protease. The fully protected fragments 74-81, 82-99 and 90-99 have been synthesized on the polystyrene-polyethylenglykol resin TentaGel, split off with dilute acetic acid and assembled in solution without loss of side-chain protecting groups. After protection of the C-terminus of the frag ment 90-99, the second fragment was coupled with TBTU/NMM. The couplings were moni tored by IS-MS and HPLC. Racemization was checked by chiral gas-chromatography on a Chirasil-Val capillary.
	Reference	Z. Naturforsch. 51b, 1339—1346 (1996); received April 10 1996
	Published	1996
	Keywords	HIV 1-Protease, Trityl-Linker, Fragment Condensation, Peptide Synthesis, Ionspray-MS, Chiral Gas-chromatography
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	TEI-XML for	default:Reihe_B/51/ZNB-1996-51b-1339.pdf
	Identifier	ZNB-1996-51b-1339
	Volume	51

10	Author	Yuejin Lia, Lianshan Zhangb, Ernst Bayerb, Dieter Oelkrugc, Ulrich Wesera	Requires cookie*
	Title	Comparative Luminescence of Rat Liver Cu-thionein and Its Chemically Synthesized a-Domain
	Abstract	A peptide corresponding to the a-dom ain o f rat liver m etallothionein-2 was chemically syn thesized employing the solid phase peptide synthesis technique. Its luminescence properties that depend on the coordinated Cu(I) have been studied using luminescence spectrometric titration in the presence o f Cu(I). Unlike the intact metallothionein which has been converted into the Cu species, the emission and excitation spectra o f the Cu-a-fragm ent showed a red shift by 20 nm and 65 nm, respectively, suggesting a more compact and stable luminophore in the a-dom ain. Saturation o f Cu(I) coordination was reached in the presence o f 6.5 mol eq Cu(I) when the a-fragment was used and 12 mol eq Cu(I) were specifically bound by the intact metallothionein. The emission bands were hom ogeneous and no decline o f the cluster struc ture was observed when excessive Cu(I) was added after saturation. A rearrangement o f the Cu-cluster in metallothionein during its formation seems to be plausible.
	Reference	Z. Naturforsch. 45c, 1193—1196 (1990); received June 6/A ugust 21 1990
	Published	1990
	Keywords	a-Fragment o f M etallothionein, Luminescence, Cu-Binding, Solid Phase, Peptide Synthesis
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	TEI-XML for	default:Reihe_C/45/ZNC-1990-45c-1193.pdf
	Identifier	ZNC-1990-45c-1193
	Volume	45