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Cyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.

Martins J, Vasconcelos V - Mar Drugs (2015)

Bottom Line: Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria.It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks.The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Sciences, University of Porto, Rua do Campo Alegre, Porto 4169-007, Portugal. joana.o.martins@gmail.com.

ABSTRACT
Cyanobacteria are considered to be one of the most promising sources of new, natural products. Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria. Among these, cyanobactins have sparked attention due to their interesting bioactivities and for their potential to be prospective candidates in the development of drugs. It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks. The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

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Cyanobactins that encode heterocyclization enzymes. The peptides are organized in chronological order and the sequence of the core peptide is presented in the linear form. The location of the prenyl-group is indicated by one letter amino acid abbreviation in the correspondent column. The genes are identified by different colors. Heterocyclization of Cys (pale yellow) or Ser/Thr (pale blue), oxidation to azole (red dashed line), prenylation (pale red) and N-methylation (pale green) are indicated in the chemical structures.
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marinedrugs-13-06910-f003: Cyanobactins that encode heterocyclization enzymes. The peptides are organized in chronological order and the sequence of the core peptide is presented in the linear form. The location of the prenyl-group is indicated by one letter amino acid abbreviation in the correspondent column. The genes are identified by different colors. Heterocyclization of Cys (pale yellow) or Ser/Thr (pale blue), oxidation to azole (red dashed line), prenylation (pale red) and N-methylation (pale green) are indicated in the chemical structures.

Mentions: Ulicyclamide and ulithiacyclamide were the first cyanobactins to be discovered by Ireland and Scheuer in 1980 (Figure 3) [6]. These small cyclic peptides isolated from the ascidian L. patella from Palau, Western Caroline Islands, unveiled a combination of chemical features, including N-to-C macrocyclization and heterocyclization to form thiazol(in)e and oxazoline motifs that were unique [2,6]. It was unclear at the time if the ascidian hosts or their partners produced these compounds, since information about chemical switches between the ascidians and their symbiotic algae was scarce [6]. Two years later, the octapeptides patellamides A, B and C were reported and isolated from L. patella collected at Eil Malk Island, Palau Islands [21]. In 1983, three new cyclic heptapeptides (1, 2 and 3) recently named lissoclinamides from L. patella were described as the first thiazoline-containing peptides isolated from this organism [22]. This work developed by Wasylyk and co-workers also presented a revised structure for ulicyclamide. In fact, in 1983, Hamamoto reported the structure of patellamide A (ascidiacyclamide) with a different skeleton [51] and later studies assigned the correct structures of ulicyclamide and patellamide A, as described by Wasylyk and Hamamoto [1,52,53]. In 1989, four novel cyclic peptides, including patellamide D and lissoclinamides 4, 5 and 6 were isolated from the same tunicate species [54,55]. The known peptides derived from L. patella were categorized in two separate groups, one constituted by ulithiacyclamide (structure determined by Biskupiak and Ireland [56]) and patellamides A, B and C and the other represented by ulicyclamide and lissoclinamides 1–3. Both groups present uncommon amino acids containing thiazole moieties, but differ in the nature of their macrocyclic ring skeleton [55]. At the same time, Williams and Moore [57] reported on the isolation and structure determination of ulithiacyclamide B from L. patella from Pohnpei, Federated States of Micronesia. The difference between ulithiacyclamide and ulithiacyclamide B is that the latter lacks the symmetry associated with ulithiacyclamide and possesses a phenyl group [57]. Patellamide E was isolated from L. patella collected in Pulau Salu, Singapore. The tunicate extract also contained patellamides A and B and ulithiacyclamide [58]. Patellamide F was characterized from the extract of L. patella sampled from northwestern Australia. The extract also contained patellamide B, ulithiacyclamide and lissoclinamide 3 [59]. In 1998, during a screening for multidrug resistance (MDR) reversing agents from marine organisms, four new cyclic peptides, assigned patellamide G and ulithiacyclamides E−G, were isolated from the tunicate L. patella collected in Pohnpei, along with the known patellamides A−C and ulithiacyclamide B. A common aspect of the novel metabolites was that at least one of the threonine units was not cyclized to an oxazoline ring [60].


Cyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.

Martins J, Vasconcelos V - Mar Drugs (2015)

Cyanobactins that encode heterocyclization enzymes. The peptides are organized in chronological order and the sequence of the core peptide is presented in the linear form. The location of the prenyl-group is indicated by one letter amino acid abbreviation in the correspondent column. The genes are identified by different colors. Heterocyclization of Cys (pale yellow) or Ser/Thr (pale blue), oxidation to azole (red dashed line), prenylation (pale red) and N-methylation (pale green) are indicated in the chemical structures.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663559&req=5

marinedrugs-13-06910-f003: Cyanobactins that encode heterocyclization enzymes. The peptides are organized in chronological order and the sequence of the core peptide is presented in the linear form. The location of the prenyl-group is indicated by one letter amino acid abbreviation in the correspondent column. The genes are identified by different colors. Heterocyclization of Cys (pale yellow) or Ser/Thr (pale blue), oxidation to azole (red dashed line), prenylation (pale red) and N-methylation (pale green) are indicated in the chemical structures.
Mentions: Ulicyclamide and ulithiacyclamide were the first cyanobactins to be discovered by Ireland and Scheuer in 1980 (Figure 3) [6]. These small cyclic peptides isolated from the ascidian L. patella from Palau, Western Caroline Islands, unveiled a combination of chemical features, including N-to-C macrocyclization and heterocyclization to form thiazol(in)e and oxazoline motifs that were unique [2,6]. It was unclear at the time if the ascidian hosts or their partners produced these compounds, since information about chemical switches between the ascidians and their symbiotic algae was scarce [6]. Two years later, the octapeptides patellamides A, B and C were reported and isolated from L. patella collected at Eil Malk Island, Palau Islands [21]. In 1983, three new cyclic heptapeptides (1, 2 and 3) recently named lissoclinamides from L. patella were described as the first thiazoline-containing peptides isolated from this organism [22]. This work developed by Wasylyk and co-workers also presented a revised structure for ulicyclamide. In fact, in 1983, Hamamoto reported the structure of patellamide A (ascidiacyclamide) with a different skeleton [51] and later studies assigned the correct structures of ulicyclamide and patellamide A, as described by Wasylyk and Hamamoto [1,52,53]. In 1989, four novel cyclic peptides, including patellamide D and lissoclinamides 4, 5 and 6 were isolated from the same tunicate species [54,55]. The known peptides derived from L. patella were categorized in two separate groups, one constituted by ulithiacyclamide (structure determined by Biskupiak and Ireland [56]) and patellamides A, B and C and the other represented by ulicyclamide and lissoclinamides 1–3. Both groups present uncommon amino acids containing thiazole moieties, but differ in the nature of their macrocyclic ring skeleton [55]. At the same time, Williams and Moore [57] reported on the isolation and structure determination of ulithiacyclamide B from L. patella from Pohnpei, Federated States of Micronesia. The difference between ulithiacyclamide and ulithiacyclamide B is that the latter lacks the symmetry associated with ulithiacyclamide and possesses a phenyl group [57]. Patellamide E was isolated from L. patella collected in Pulau Salu, Singapore. The tunicate extract also contained patellamides A and B and ulithiacyclamide [58]. Patellamide F was characterized from the extract of L. patella sampled from northwestern Australia. The extract also contained patellamide B, ulithiacyclamide and lissoclinamide 3 [59]. In 1998, during a screening for multidrug resistance (MDR) reversing agents from marine organisms, four new cyclic peptides, assigned patellamide G and ulithiacyclamides E−G, were isolated from the tunicate L. patella collected in Pohnpei, along with the known patellamides A−C and ulithiacyclamide B. A common aspect of the novel metabolites was that at least one of the threonine units was not cyclized to an oxazoline ring [60].

Bottom Line: Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria.It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks.The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Sciences, University of Porto, Rua do Campo Alegre, Porto 4169-007, Portugal. joana.o.martins@gmail.com.

ABSTRACT
Cyanobacteria are considered to be one of the most promising sources of new, natural products. Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria. Among these, cyanobactins have sparked attention due to their interesting bioactivities and for their potential to be prospective candidates in the development of drugs. It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks. The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

Show MeSH
Related in: MedlinePlus