Isolation of RP 71955, a new anti-HIV-1 peptide secondary metabolite.

Helynck, G.; Dubertret, Catherine; Mayaux, Jean‐François; Leboul, J.

doi:10.7164/antibiotics.46.1756

Cited by 56 publications

(52 citation statements)

References 5 publications

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“…The anantin type, such as anantin (Wyss et al 1991), RES-701s (Yano et al 1996;Yamasaki et al 1994), propeptin (Kimura et al 2007), BI-32169 (Potterat et al 2004), and capistruin (Knappe et al 2008), has an internal linkage between the α-amino group of Gly1 and the γ-carboxyl group of Asp8 or Asp9. The siamycin type including siamycins (Detlefsen et al 1995) and aborycin (Helynck et al 1993) has an internal linkage between the α-amino group of Cys1 and the β-carboxyl group of Asp9 and two additional disulfide bridges between Cys1 and Cys13 and between Cys7 and Cys19.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Inokoshi

Matsuhama

Miyake

et al. 2012

Appl Microbiol Biotechnol

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The biosynthetic gene cluster for lariatins A and B, anti-mycobacterial peptide antibiotics with a unique "lasso" structure, was cloned from Gram-positive bacterium Rhodococcus jostii K01-B0171. Random transposition mutagenesis using IS1415 derivative was carried out to identify a chromosomal locus involved in lariatin biosynthesis and six independent lariatin non-producing variants were obtained. Arbitrary PCR revealed that one insertion was located near the region involved in lariatin biosynthesis. Using the lariatin gene as a probe, a genomic library of R. jostii K01-B0171 was screened by colony hybridization, and two clones were obtained. Sequence analysis of these clones revealed that the gene cluster for lariatin biosynthesis spanning about 4.5 kb consisted of five open reading frames (larA to larE). We proposed that the linear precursor LarA is processed by LarB, LarC, and LarD, and the mature lariatin is exported by LarE.

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Section: Introductionmentioning

confidence: 99%

Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Inokoshi

Matsuhama

Miyake

et al. 2012

Appl Microbiol Biotechnol

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“…To this solution was added NH 4 PF 6 (114 mg, 0.7 mmol, 5 equiv) and H 2 O milliQ (5 mL): the biphasic solution was stirred vigorously for 30 minutes. The aqueous layer was then extracted with CH 2 Cl 2 (3 × 5 mL) and the combined organic layers were dried over MgSO 4 …”

Section: Synthesis and Characterizations Of [1]rotaxanes 13 And 14mentioning

confidence: 99%

“…They also described the resistance of the obtained peptide rotaxane against enzyme-catalyzed hydrolysis depending on the photoisomerization of the diazo moiety [40]. Meanwhile, Smithrud et al designed rotaxanes as peptide carriers, using a grafted crown ether and a calix [4]arene, cyclophane, or cleft as a blocking group [41]. It remains from all these studies that protection of peptides against enzymatic degradation, on one hand, and the tailoring of the shape of peptides, on another hand, are two main problems to tackle for the conception of new efficient peptide drugs.…”

Section: Introductionmentioning

confidence: 99%

“…The encircled peptide axle then adopts a looped conformation, conferring to the lasso a very compact tridimensional structure, which is responsible for its biological activity. Beyond their remarkable stability against proteolytic degradation, chemical and thermal denaturation [1][2][3], some lasso peptides proved to inhibit HIV replication [4] or the Gram-negative RNA polymerase [5]. As a particular example of lasso peptide, the ribosomally synthesized [6,7] antimicrobial peptide microcin J25 (MccJ25), which was isolated from E. coli in 1992, [8] has been extensively studied during the past years [9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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A pH-Sensitive Peptide-Containing Lasso Molecular Switch

2013

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Abstract:The synthesis of a peptide-containing lasso molecular switch by a selfentanglement strategy is described. The interlocked [1] rotaxane molecular machine consists of a benzometaphenylene [25]crown-8 (BMP25C8) macrocycle surrounding a molecular axle. This molecular axle contains a tripeptidic sequence and two molecular stations: a N-benzyltriazolium and a pH-sensitive anilinium station. The tripeptide is located between the macrocycle and the triazolium station, so that its conformation can be tailored depending on the shuttling of the macrocycle from one station to the other. At acidic pH, the macrocycle resides around the anilinium moiety, whereas it shuttles around the triazolium station after deprotonation. This molecular machinery thus forces the lasso to adopt a tightened or a loosened conformation.

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“…[4][5][6][7] Some of the known lasso peptides are secreted into the surrounding media. [8,9] Their proposed biological role is to act as antibacterial agents, presumably to give advantage over competing bacterial species or strains within the same habitat. The peptides were isolated from various microbial sources, including Streptomyces strains, Rhodococcus, Microbispora and Escherichia coli and identified as potent inhibitors of various pharmaceutically relevant receptors.…”

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confidence: 99%