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  • 1
    Electronic Resource
    Electronic Resource
    Optimization of capillary electrophoresis of mixtures of basic peptides and comparison with HPLC (1993)
    s.l. : American Chemical Society
    Analytical chemistry 65 (1993), S. 1399-1405 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac00058a016
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  • 2
    Electronic Resource
    Electronic Resource
    A rational approach for the development of reduced-size analogues of neuropeptide Y with high affinity to the Y1 receptor (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 341-348 
    Details
    ISSN: 1075-2617
    Keywords: Neuropeptide Y ; centrally truncated analogues ; Y1 receptor binding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Four sets of centrally truncated analogues of neuropeptide Y have been synthesized. In each series the N-terminal part was constant, while the C-terminal segment was systematically varied in length. The C- and N-terminal parts were linked by 6-aminohexanoic acid. The affinity to the Y1 receptor was investigated on human neuroblastoma cells SK-N-MC. Significant differences were found between the series of peptides as well as within each set. Remarkably, the affinity did not solely depend on the length of the segment, and with increasing numbers of residues the IC50 values were not always decreased. With a given N-terminal segment, only one optimal length of the C-terminal segment was found, which suggests that it is not the amino acids themselves but their 3D arrangement and orientation that is important for high receptor affinity.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010509
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  • 3
    Electronic Resource
    Electronic Resource
    Synthetic S-(2,3-dihydroxypropyl)-cysteinyl peptides derived from the N-terminus of the cytochrome subunit of the photoreaction centre of Rhodopseudomonas viridis enhance murine splenocyte proliferation (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 184-190 
    Details
    ISSN: 1075-2617
    Keywords: Immunomodulators ; lipopeptides ; peptide synthesis ; S-[2,3-dihydroxypropyl]-cysteine ; splenocyte activators ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Various lipopeptides representing the N-terminal part of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas virdis were prepared by solid-phase peptide synthesis. These lipopeptides consisted of a S-[2,3-dihydroxypropyl]-cysteinyl (Dhc) residue N-terminally coupled to the nonapeptide FEPPPATTT. Different numbers of palmitoyl (Pam) chains were attached to Dhc via ester and/or amide bonds. The lipopeptide Dhc(Pam)2-FEPPPATTT containing two ester-bonded palmitoyl residues and a free N-chain lipopeptide Pam-Dhc(Pam)-FEPPPATTT containing one amide- and one ester-bonded palmitoyl residues, the two-chain lipopeptide Pam-Dhc(Pam)-FEPPPATTT containing one amide- and one ester-bonded palmitoyl residue, and the N-terminally elongated lipopeptide SLVAG-Dhc(Pam)2-FEPPPATTT were less active. The nonapeptide FEPPPATTT and the decapeptide Dhc-FEPPPATTT were only merginal splenocyte activators, even at concentrations as high as 1 μM. Thus, lipopeptide Dhc(Pam)2-FEPPPATTT constitutes the first potent splenocyte stimulating Dhc-lipopeptide described so far that contains only two fatty acid residues.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010305
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  • 4
    Electronic Resource
    Electronic Resource
    Anchor-linked intermediates in peptide amide synthesis are caused by dimeric anchors on the solid supports (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 191-200 
    Details
    ISSN: 1075-2617
    Keywords: Peptide amide ; amide anchors ; intermediates in peptide amide synthesis ; cleavage of peptide amides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Cleavage and kinetic studies have been carried out using commercially obtained H-Tyr(tBu)-5-(4′-aminomethyl-3′,5′-dimethoxyphenoxy)valeric acid-TentaGelS (H-Tyr(tBu)-4-ADPV-TentaGelS) and H-Tyr (tBu)-4-ADPV-Ala-aminomethyl-resin (H-Tyr(tBu)-4-ADPV-AM-resin) prepared from commercially available resin and loaded with commercially available Fmoc-4-ADPV-OH amide anchor. Cleavage with pure trifluoroacetic acid (TFA) gave the intermediate H-Tyr-4-ADPV-NH2, which was then degraded to H-Tyr-NH2, and cleavage with TFA/dichloromethane (1:9) yielded H-Tyr-4-ADPV-NH2 which could be isolated in preparative amounts. Cleavage reactions with 15N-labelled H-Ala-4-ADPV-[15N]-Gly-AM-resin yielded the intermediate H-Ala-4-ADPV-NH2, which contained no 15N as demonstrated by 1H-NMR. The analysis of the commercial Fmoc-4-ADPV-OH amide anchor showed the presence of Fmoc-4-ADPV-4-ADPV-OH as an impurity in high amounts. This dimeric anchor molecule is the cause of formation of the anchor-linked peptide intermediate obtained during the cleavage from the resin. The particularly high acid-lability of the amide bond between the two ADPV moieties was utilized to synthesize sidechain and C-terminally 4-ADPV protected pentagastrin on a double-anchor resin, and to cleave it using 5% trifluoroacetic acid in dichloromethane. This method may offer a new way for the synthesis of protected peptide amides with improved solubility to be used in fragment condensation.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010306
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  • 5
    Electronic Resource
    Electronic Resource
    A new approach to secondary structure evaluation: Secondary structure prediction of porcine adenylate kinase and yeast guanylate kinase by CD spectroscopy of overlapping synthetic peptide segments (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 213-231 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new approach for evaluating the secondary structure of proteins by CD spectroscopy of overlapping peptide segments is applied to porcine adenylate kinase (AK1) and yeast guanylate kinase (GK3).One hundred seventy-six peptide segments of a length of 15 residues, overlapping by 13 residues and covering the complete sequences of AK1 and GK3, were synthesized in order to evaluate their secondary structure composition by CD spectroscopy.The peptides were prepared by solid phase multiple peptide synthesis method using the 9-fluorenylmethoxycarbonyl/tert-butyl strategy. The individual peptide secondary structures were studied with CD spectroscopy in a mixture of 30% trifluoroethanol in phosphate buffer (pH 7) and subsequently compared with x-ray data of AK1 and GK3.Peptide segments that cover α-helical regions of the AK1 or GK3 sequence mainly showed CD spectra with increasing and decreasing Cotton effects that were typical for appearing and disappearing α-helical structures. For segments with dominating β-sheet conformation, however, the application of this method is limited due to the stability and clustering of β-sheet segments in solution and due to the difficult interpretation of random-coiled superimposed β-sheet CD signals.Nevertheless, the results of this method especially for α-helical segments are very impressive. All α-helical and 71% of the β-sheet containing regions of the AK1 and GK3 could be identified. Moreover, it was shown that CD spectra of consecutive peptide content reveal the appearance and disappearance of α-helical secondary structure elements and help localizing them on the sequence string. © 1997 John Wiley & Sons, Inc. Biopoly 41: 213-231, 1997
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Structure-activity relationships of neuropeptide Y analogues with respect to Y1 and Y2 receptors (1995)
    New York : Wiley-Blackwell
    Biopolymers 37 (1995), S. 123-142 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Secondary structure investigations, affinities, and activities of neuropeptide Y analogues with respect to the Y1 and the Y2 receptor are reviewed. The results are discussed with respect to the different prerequisites for affinities to both receptor subtypes. The results from a systematic scanning of the hormone using L-alanine and from a large variety of discontinuous and cyclic analogs suggest that two different conformations of neuropeptide Y are adopted at the Y1 and Y2 receptors. Whereas a C-terminal turn structure is suggested for Y1 receptor affinity, an α-helical conformation of the C-terminus is afforded for good binding to the Y2 receptor. © 1994 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360370207
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  • 7
    Electronic Resource
    Electronic Resource
    α-Helical small molecular size analogues of neuropeptide Y: Structure-activity relationships (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 613-619 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: C-terminal analogues of neuropeptide Y (NPY) of small molecular size have been synthesized. The influence of chain length, single or multiple amino acid substitution, and segment substitutions on receptor binding, pre- and postsynaptic biological activity, and conformational properties have been investigated. Receptor binding and in vivo assays revealed biological activity for NPY Ac-25-36 that increased with increasing α-helicity. In attempts to stabilize the α-helical content, three independent types of modified NPY Ac-25-36 analogues were synthesized. Strong agonistic activities could be detected in a series of discontinuous analogues, which are constructs of N-terminal parts linked via different spacer molecules to C-terminal segments. One of the most active molecules was NPY 1-4-Aca-25-36 (Aca, ε-aminocaproic acid). For the first time conformational properties of a series of small NPY analogues have been investigated by CD, and correlated with biological activity and receptor binding. A C-terminal dodecapeptide segment of NPY with an amount of 50% substitution to the native C-terminal sequence of NPY was found to exhibit significant receptor binding.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310605
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  • 8
    Electronic Resource
    Electronic Resource
    Methoden der multiplen Peptidsynthese und ihre AnwendungenProfessor Ernst Bayer zum 65. Geburtstag gewidmet (1992)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 104 (1992), S. 375-391 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die rasch fortschreitende Entwicklung in der Biotechnologie neuer Proteine, in der Immunologie und in der auf Inhibitoren und Antagonisten basierenden Pharmaforschung führen zu einem immensen Bedarf an synthetischen Peptiden. Durch multiple Methoden können heute 100-150 völlig verschiedene Peptide mit Kettenlängen bis etwa 20 Aminosäuren gleichzeitig hergestellt werden. Die erzielten Ausbeuten und Qualitäten reichen aus, um ein verläßliches Screening auf biologische Aktivität in vitro und in vivo durchzuführen; dasselbe gilt für Syntheseoptimierungen, Sekundärstrukturvergleiche und Konformationskartierungen. Mit speziellen multiplen Methoden gelingt die Epitopkartierung auch größerer Proteine zur Diagnostik und Impfstoffentwicklung anhand von einigen hundert freien oder an Stäbchen gebundenen Peptiden, die für Immunoassays einsetzbar sind. Multiple Methoden der Peptidsynthese ermöglichen auch den Aufbau von sogenannten Peptidbibliotheken. Diese können Hunderttausende von Peptiden umfassen, wodurch sich neue Perspektiven für das Screening nach Leitstrukturen eröffnen. Mit einer speziellen Peptidsynthese, die die Verwendung von photolabilen Schutzgruppen und photolithographischen Verfahren kombiniert, können Peptidbibliotheken auf Plättchen für miniaturisierte Immunoassays aufgebaut werden. Lipopeptid-Anti-gen-Konjugate, die komplette Proteinsequenzen aus überlappenden Peptidsegmenten umfassen, machen die Herstellung peptidspezifischer und monoklonaler Antikörper sowie ein gezieltes Screening auf Epitope von B-, T-Helfer- und T-Killer-Zellen möglich. Anwendungen auf dem Gebiet der AIDS-Diagnostik, der Impfstoffentwicklung, oder dem Screening nach Hormonanaloga demonstrieren die Perspektiven, die sich durch die multiplen Synthesemethoden eröffnen.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19921040404
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  • 9
    Electronic Resource
    Electronic Resource
    Investigations on different coupling reagents for the synthesis of a cyclopeptide analog of neuropeptide Y (1991)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1991 (1991), S. 585-590 
    Details
    ISSN: 0170-2041
    Keywords: Cyclization methods ; Neuropeptide Y ; Coupling reagents ; Cyclopeptide ; Peptide synthesis ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The short-cut analog of neuropeptide Y (NPY), NPY 1YESK-Ahx-25RHYINKITRQRY-NH2, was synthesized on the amide anchor 5-(4-aminomethyl-3,5-dimethoxyphenoxy)valeric acid (ADPV) attached to polystyrene/1% divinylbenzene by using the 9-fluorenylmethoxycarbonyl/tert-butyl (Fmoc/tBu) strategy. Side-chain-to-side-chain cyclization of residues Glu2 to Lys30 of this linear heptadecapeptide amide was carried out by using different activating reagents under high-dilution conditions of the free peptide. The use of diphenylphosphoryl azide (DPPA) with the addition of triethylamine gave the highest yield of cyclic peptide. Replacing the tertiary amine by dipotassium hydrogen phosphate as an insoluble inorganic base did not improve the cyclization. Complete cyclization was achieved within four hours by using 2-(1H-benzotriazol-1-yl) -1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) in combination with 1-hydroxybenzotriazol (HOBt) as activating agent, but the separation from excess TBTU resulted in lower yields. Reactions were monitored by HPLC and kinetic investigations were made. The identity and purity of the final product were proven by various analytical methods including atmospheric pressure ionization mass spectrometry (API-MS). The receptor binding constant of the cyclic analog was found to be comparable to that of NPY.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.1991199101106
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  • 10
    Electronic Resource
    Electronic Resource
    Synthesis and Conformational Analysis by CD Spectroscopy of Lantibiotic Leader, Pro- and Pre-Peptides (1993)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1993 (1993), S. 1125-1131 
    Details
    ISSN: 0170-2041
    Keywords: Lantibiotics ; Circular dichroism ; Gallidermin ; Percursor proteins ; Conformation ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In order to investigate the conformational properties of the precursor proteins of lanthionine-containing bacteriocins we synthesized the leader peptides of the pre-lantibiotics of gallidermin, epidermin, Pep5, nisin, subtilin, the C-terminal 30-mer segment of pre-cinnamycin, propeptide segments of Pep5 and gallidermin and the complete pre-gallidermin, which consists of 52 residues. The peptides were synthesized in a step-by-step synthesis by the Fmoc/tBu strategy using an optimized procedure for the synthesis of large peptides. All peptides were analyzed by HPLC and characterized by electrospray mass spectrometry and amino acid analysis. Circular dichroism spectra exhibited strong α-helical Cotton effects even at a low concentration of trifluoroethanol for all N-terminal leader peptides. Comparative investigations of the C-terminal propeptide segments led to a model of the conformation of the prepeptides of Pep5 and gallidermin in aqueous and lipophilic environments. In addition, circular dichroism investigations on the synthetic precursor protein of gallidermin and the isolated natural pre-Pep5 were performed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.1993199301180
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