A novel cyclotetrapeptide produced by Lactobacillus helveticus as a tyrosinase inhibitor

Kawagishi, Hirokazu; Somoto, Akishige; Kuranari, J.; Kimura, Atsuo; Chiba, Seiya

doi:10.1016/s0040-4039(00)79177-5

Cited by 48 publications

(42 citation statements)

References 3 publications

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“…This is in accordance with the prediction of conformations performed by molecular mechanics calculations [12]. The influence of the Ch-configuration in Pro-containing peptides is also illustrated by unsuccessful syntheses [8] of cyclo(Pro-VaL-Pro-Tyr) [13] and the difficult synthesis of cyclo(Pro-Val) 2 [14]. Even the attempted synthesis of cyclo(Pro-Gly) 2 , in which L-Pro residues alternate with Gly residues, which is assumed to promote cyclization, failed [15] since the cyclization of the precursor Gly-Pro-Gly-Pro-pnitrophenyl ester resulted in a mixture of cyclo(Pro-Gly) 4 and Pro-Gly diketopiperazine cyclo(Pro-Gly) 1 .…”

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confidence: 87%

All-L-Leu-Pro-Leu-Pro: a challenging cyclization

et al. 2000

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In this paper, we report the difficult synthesis of cyclo(Leu‐Pro‐Leu‐Pro). While the cyclization of Leu‐Pro‐Leu‐D‐Pro did not cause problems, the all‐L‐peptide afforded cyclodimer rather than cyclotetrapeptide (cyclomonomer). A first attempt using our reversible backbone substitution methodology failed. However, we were successful in obtaining the desired cyclo(Leu‐Pro‐Leu‐Pro) by decreasing the concentration. The ratio of cyclomonomer to cyclodimer was raised to 1:1.1 using BOP and 1:0.6 using HATU under our high dilution condition. The structures of the cyclopeptides were confidently assigned by electrospray ionization mass spectrometry and NMR. Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.

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confidence: 87%

All-L-Leu-Pro-Leu-Pro: a challenging cyclization

et al. 2000

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“…Further, a novel cyclic tetrapeptide isolated from a Pseudomonas sp. (strain IM-1) associated with the marine sponge Ircinia muscarum was found to contain two proline units, one with l -configuration and the other with d -configuration [77]. …”

Section: Chemistrymentioning

confidence: 99%

Natural Proline-Rich Cyclopolypeptides from Marine Organisms: Chemistry, Synthetic Methodologies and Biological Status

et al. 2016

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Peptides have gained increased interest as therapeutics during recent years. More than 60 peptide drugs have reached the market for the benefit of patients and several hundreds of novel therapeutic peptides are in preclinical and clinical development. The key contributor to this success is the potent and specific, yet safe, mode of action of peptides. Among the wide range of biologically-active peptides, naturally-occurring marine-derived cyclopolypeptides exhibit a broad range of unusual and potent pharmacological activities. Because of their size and complexity, proline-rich cyclic peptides (PRCPs) occupy a crucial chemical space in drug discovery that may provide useful scaffolds for modulating more challenging biological targets, such as protein-protein interactions and allosteric binding sites. Diverse pharmacological activities of natural cyclic peptides from marine sponges, tunicates and cyanobacteria have encouraged efforts to develop cyclic peptides with well-known synthetic methods, including solid-phase and solution-phase techniques of peptide synthesis. The present review highlights the natural resources, unique structural features and the most relevant biological properties of proline-rich peptides of marine-origin, focusing on the potential therapeutic role that the PRCPs may play as a promising source of new peptide-based novel drugs.

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“…The following characteristic structural features can be recognised in naturally occurring cyclotetrapeptides: (i) three L-and one D-amino acids in cancerostatic cyclopeptides of the chlamydocin group (2-6); (ii) three L-amino acids and one dehydroamino acid in the tentoxin ring (7); (iii) four L-amino acids in the tyrosine inhibitor cyclo (Pro-Val-Pro-Val) (8) and in the three cancerostatic cyclopeptides cyclo(Pro-Leu),, cyclo(Pro-Val), and cyclo(Pro-Phe), isolated from a tunicate of the family Didemnidae (9); four L-amino acids with three amide and one amidine bond in bottromycin (lo).…”

Section: Cyclotetrapeptidesmentioning

confidence: 99%

Cyclotetrapeptides and cyclopentapeptides: occurrence and synthesis*

Schmidt

Langner

1997

The Journal of Peptide Research

123

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The structures reported for the three cancerostatic all‐l‐cyclotetrapeptides cyclo(Pro‐Leu)2, cyclo(Pro‐Val)2 and cyclo(Pro‐Phe)2 isolated from a tunicate seem questionable. The synthetic compounds claimed to be identical to the naturally occurring cyclotetrapeptides are in fact not cyclotetrapeptides but rather cyclooctapeptides. We have not been able to prepare the tyrosinase inhibitor cyclo(Pro‐Val‐Pro‐Tyr). Ring closure of H‐Pro‐Val‐Pro‐Tyr‐OC6F5 gave rise to 31% of cyclo(Pro‐Val‐Pro‐d‐Tyr). The same product was obtained in 53% yield from H‐Pro‐Val‐Pro‐d‐Tyr‐oc6F5. For the ring closure to the all‐l‐cyclopentapeptide cyclo(Pro‐Ala‐Ala‐Phe‐Leu), all ring closure positions have been investigated. The reaction at the nitrogen atom of leucine leads to 21% of the all‐l‐cyclopentapeptide. Dimers or mixtures of monomers and dimers result from reaction at all other positions. © Munksgaard 1997.

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A novel cyclotetrapeptide produced by Lactobacillus helveticus as a tyrosinase inhibitor

Cited by 48 publications

References 3 publications

All-L-Leu-Pro-Leu-Pro: a challenging cyclization

All-L-Leu-Pro-Leu-Pro: a challenging cyclization

Natural Proline-Rich Cyclopolypeptides from Marine Organisms: Chemistry, Synthetic Methodologies and Biological Status

Cyclotetrapeptides and cyclopentapeptides: occurrence and synthesis*

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