Solid-phase synthesis of tryptophan-containing peptides

Ohno, Motonori; Tsukamoto, Sadaji; Izumiya, Nobuo

doi:10.1039/c39720000663

Cited by 14 publications

(4 citation statements)

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“…The synthesis of L * Leu5-GA was carried out by the method of solidphase peptide synthesis ( 11) with a few modifications as described earlier from this laboratory (2,12,13). In the present synthesis, the j-indole ring of the Trp residues was protected by a formyl group (14,15) to prevent air oxidation under acidic conditions. After the synthesis was completed, the N-protected peptide was removed from the resin by ethanolamine treatment and under these conditions the NI(Ie-formyl group on tryptophyl residue was also removed.…”

Section: Synthesismentioning

confidence: 99%

The source of the dispersity of gramicidin A single-channel conductances. The L X Leu5-gramicidin A analog

Urry¹,

Alonso²,

Venkatachalam³

et al. 1984

Biophysical Journal

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The L * Leu5-gramicidin A analog has been designed, synthesized, and verified for the purpose of testing the perspective that different side-chain distributions are responsible for the dispersity of single-channel conductances. The structural analysis shows that the L * Leu5 analog would limit the possible number of side-chain distributions and that the dispersity of channel conductances would decrease. The finding is the expected decrease in less probable conductance states and the associated increase in the probability of the most probable conductance state.

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Section: Synthesismentioning

confidence: 99%

The source of the dispersity of gramicidin A single-channel conductances. The L X Leu5-gramicidin A analog

Urry¹,

Alonso²,

Venkatachalam³

et al. 1984

Biophysical Journal

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“…Radioactive iodination of this partially protected human RLF by the chloramine T method (18) could be performed without oxidative degradation of the crucial tryptophan side chain (4,19). After reduction of excess oxidant with thiosulfate, the indole group was liberated by treatment with aqueous piperidine (20) (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

Specific, High Affinity Relaxin-like Factor Receptors

Büllesbach

Schwabe

1999

Journal of Biological Chemistry

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The relaxin-like factor (RLF) is a circulating hormone that binds to specific membrane-bound uterine receptors in the mouse. Mono-iodinated RLF tracers were produced and characterized specifically to study the properties of the RLF receptor. The tracers bound to the RLF receptor in uterine crude membrane preparations with high affinity (73 nM for 125 I-Tyr(A9) RLF and 90 nM for 125 I-Tyr(A26) RLF) as determined by Scatchard analysis. The specificity of binding was confirmed by chemical cross-linking experiments. Binding of 125 I-Tyr(A9) RLF to the putative receptor was inhibited in the presence of a 640-fold excess of unlabeled human RLF but not by the same excess of human relaxin. SDS-gel electrophoresis of the RLF-receptor complex revealed a molecular mass of >200 kDa, which remained unchanged upon reduction. The size and the lack of subunit structure of the receptor is similar to the features reported for the relaxin receptor. In this regard both, the RLF and the relaxin receptor are different from the insulinand the insulin-like growth factor-type 1 receptors. This observation supports the relaxin-likeness of this new factor not only toward potential target tissues but also as regards receptor features.The relaxin-like factor (RLF) 1 is synthesized in gonadal tissues of males and females. The mRNA was first detected in Leydig cells and named, accordingly, Leydig insulin-like peptide (LEY I-L) (1). Later distinct but low levels of RLF mRNA were detected in female tissues, i.e. human trophoblasts (2), human corpora lutea (2), and mouse ovaries (3). The location of RLF expression implied a potential physiological role in reproduction and thereby a functional relatedness to relaxin rather than to insulin. This impression was reinforced when the protein was synthesized so that it seemed appropriate to adopt the name relaxin-like factor (RLF) (4).In humans RLF is a circulating hormone with higher levels in post-puberty males than in children and post-puberty females (5). This is in agreement with the relative expression levels in gonadal tissue during development in the mouse (3). The potential activity of RLF in reproduction is supported by the observation that transcription of the gene is mediated by the steroidogenic factor-1 (6) and by experiments with knockout mice in which males without a functional RLF gene are sterile because of premiotic arrest of the sperm maturation process; female knock-out mice did not show defects (7). The role of RLF in the female remains to be elucidated. The fact that RLF expression is cycle-dependent in some animals and that the mRNA is present during pregnancy (3, 8, 9) as well as the presence of RLF-specific receptors in mouse uteri again hint at a potential function in reproduction (4).The structure of human RLF as predicted from its cDNA has two chains and a disulfide bonding pattern characteristic of the relaxin/insulin family (1, 10). Human RLF, synthesized according to this prediction (4) served to elicit production of structurespecific polyclonal antibodies in rabbits t...

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“…HCUHCOOH deprotection (P.111) 191 [31]. BOC-and OtBu-protecting groups were removed by treating the peptide under NZ with a solution of 0 .…”

Section: Experimental Partmentioning

confidence: 99%

ChemInform Abstract: α‐MELANOTROPIN LABELED AT ITS TYROSINE2 RESIDUE: SYNTHESIS AND BIOLOGICAL ACTIVITIES OF 3′‐IODOTYROSINE2‐,3′‐125IODOTYROSINE2‐,3′,5′‐DIIODOTYROSINE2‐, AND (3′,5′‐3H2)TYROSINE2‐α‐MELANOTROPIN, AND OF RELATED PEPTIDES

Eberlé¹,

Huebscher²

1980

Chemischer Informationsdienst

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Summarya-MSH was labelled at its tyrosine' residue with tritium and iodine. Several synthetic routes were investigated by preparing 13 precursor or model compounds and 4 different labelled products (via about 40 intermediates). Their melanotropic activity was determined with an in vitro frog skin assay and, for some of the compounds, with a tyrosinase assay. The tritiation was performed on [Tyr (IJ2]u-MSH by catalytic halogedtritium exchange, yielding a-MSH of high specific radioactivity (34 Ci/mmol) and full biological activity. Iodination was studied in detail using five different techniques. An equimolar chloramine T procedure proved to be the most convenient and reproducible method, resulting in monoiodinated u-MSH containing 99% of the label in position 2. The biological activity was 50% that of a-MSH; the specific radioactivity, determined in a competitive binding assay with a highly specific a-MSH antiserum and [Tyr(I)']a-MSH as competitor, was 1530 Ci/mmol. The labelling techniques and the biological results are discussed.Introduction. -Recent findings of a possibly decisive involvement of a-melanotropin (a-MSH) in neural functioning and foetal development are the reason for renewed intense investigation of this tridecapeptide [3]. From synthetic studies on structure/function relations it appeared that different target cell receptors may recognize different portions of the a-MSH molecule [4]. In order to study such hormone-receptor interactions in more detail, a-MSH derivatives are synthesized which

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Solid-phase synthesis of tryptophan-containing peptides

Cited by 14 publications

References 0 publications

The source of the dispersity of gramicidin A single-channel conductances. The L X Leu5-gramicidin A analog

The source of the dispersity of gramicidin A single-channel conductances. The L X Leu5-gramicidin A analog

Specific, High Affinity Relaxin-like Factor Receptors

ChemInform Abstract: α‐MELANOTROPIN LABELED AT ITS TYROSINE2 RESIDUE: SYNTHESIS AND BIOLOGICAL ACTIVITIES OF 3′‐IODOTYROSINE2‐,3′‐125IODOTYROSINE2‐,3′,5′‐DIIODOTYROSINE2‐, AND (3′,5′‐3H2)TYROSINE2‐α‐MELANOTROPIN, AND OF RELATED PEPTIDES

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