Peptídeos cíclicos de biomassa vegetal: características, diversidade, biossíntese e atividades biológicas

Picchi, Douglas Gatte; Altei, Wanessa Fernanda; Saito, Mônica Sue; Bolzani, Vanderlan da Silva; Cilli, Eduardo Maffud

doi:10.1590/s0100-40422009000500033

Cited by 12 publications

(19 citation statements)

References 83 publications

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“…CPs belonging to the Caryophyllaceae group consist of 7-10 aminoacids with a high proportion of hydrophobic residues [8][9][10][11][12] being recently named as Orbitide [13]. Biobollein (9 residues) and Labaditin (10 residues), isolated from Jatropha Multifida, were the first CPs of this group of peptides described in the literature [8,14,15].…”

Section: Introductionmentioning

confidence: 99%

Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

Barbosa

Cilli

Dias

et al. 2015

Journal of Colloid and Interface Science

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Conformational changes of the cyclic (Lo) peptide Labaditin (VWTVWGTIAG) and its linear analogue (L1) promoted by presence of anionic sodium dodecyl sulfate (SDS) and zwitterionic L-α-Lysophosphatidylcholine (LPC) micelles were investigated. Results from λ(max) blue-shift of tryptophan fluorescence emission combined with Stern-Volmer constants values and molecular dynamics (MD) simulations indicated that L1 interacts with SDS micelles to a higher extent than does Lo. Further, the MD simulation demonstrated that both Lo and L1 interact similarly with LPC micelles, being preferentially located at the micelle/water interface. The peptide-micelle interaction elicits conformational changes in the peptides. Lo undergoes limited modifications and presents unordered structure in both LPC and SDS micelles. On the other hand, L1 displays a random-coil structure in aqueous medium, pH 7.0, and it acquires a β-structure upon interaction with SDS and LPC, albeit with structural differences in each medium.

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Section: Introductionmentioning

confidence: 99%

Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

Barbosa

Cilli

Dias

et al. 2015

Journal of Colloid and Interface Science

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“…The enhancer activity however, reserved to the cyclic form (Cp), should be supported, as least in part, by the higher resistance to enzymatic hydrolysis in a medium highly hydrolytic. Even, in linear sequences ending points are suitable sites of recognition for degradation that does not occur in closed sequences [21,28]. Therefore our proposal remains to be probed.…”

Section: Biological Functions and Applicationsmentioning

confidence: 95%

“…Many reports in literature have showed that linear and cyclic peptides exhibit functional differences which are attributed to its individual structural arrangement [21]. For this reason, both synthetic peptides, linear (1341.36 g/mol) and cyclic (1323.19 g/mol), designed on the APTLSGGSVPRDAD sequence, were acquired and studied.…”

Section: Structural Analyses Of Synthetic Analoguesmentioning

confidence: 99%

A new peptide from Jatropha curcas seeds: Unusual sequence and insights into its synthetic analogue that enhances proteolytic activity of papain

Jucá

Monteiro-Moreira

Moreira

et al. 2015

Process Biochemistry

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Please cite this article in press as: Jucá TL, et al. A new peptide from Jatropha curcas seeds: Unusual sequence and insights into its synthetic analogue that enhances proteolytic activity of papain. Process Biochem (2015), http://dx. a b s t r a c tA new peptide (1341 g/mol) from Jatropha curcas seeds was isolated. The linear sequence (APTLSG-GSVPRDAD) was deduced by de novo peptide sequencing, and further used as scaffold for synthesis of linear (1342 g/mol) and cyclic (1324 g/mol) synthetic analogues. The full peptide sequence was identified as inserted in a putative conserved domain of late-embryogenesis proteins which produced a significant alignment hit (100% of identity and E-value of 1e−05) with a hypothetical protein JCGZ 12502 of J. curcas. Whereas in the linear peptide predominated the double charged ion state (m/z 671.68), in the cyclic form was observed the mono charged ion state (m/z of 1325.19) and an unusual MS/MS fragmentation pattern. The differences between the forms were discrete in terms of ionic mobility, retention time (reverse phase) and net charge as function of pH. Circular dichroism spectra presented an intense negative peak at 198 nm which is assigned for its disordered contents. A negative peak at 222 nm in the spectrum of the circular form suggested its structure was not as disordered as the linear form. The peptides were neither haemolytic nor cytotoxic and did not inhibit phytopathogenic fungi. Surprisingly, the circular but not the linear peptide increased the proteolytic activity of papain.

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“…They have been documented in families including Annonaceae, Euphorbiaceae, Lamiaceae, Linaceae, Phytolaccaceae, Rutaceae, Schizandraceae and Verbenaceae. [2][3][4][5] In recent decades, the Jatropha genus (Euphorbiaceae family) has emerged as a rich source of bioactive orbitides. 5,6 Plants from this genus are endemic in the Brazilian semi-arid region (Caatinga biome) 7 and represent a popularly known source of toxins and medicines.…”

Section: Introductionmentioning

confidence: 99%

Linear Peptide Analogues from Jatropha’s Orbitides Promote Migration of Human Neonatal Foreskin Fibroblasts in vitro and Collagen Deposition

Ramalho

Pinto

Andricopulo

et al. 2019

J. Braz. Chem. Soc.

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Orbitides are a class of small naturally occurring cyclic peptides with structural and functional diversities. Their chemical properties make this class feasible to be obtained by solid phase peptide synthesis (SPPS). Therefore, this synthetic accessibility enables useful application and facilitates the identification of analogues, bioactivity studies, and thus, enables them to be applied to obtain peptide libraries. The aim of this work was to investigate the effects of orbitides and their linear synthetic analogues on the migration of neonatal human foreskin fibroblasts. The screening of linear peptide analogues, originally designed from natural orbitides isolated from Jatropha species, demonstrated that some molecules (linear pohlianin B and linear ribifolin) have the potential to induce fibroblast migration and collagen deposition and may thus contribute to accelerating the processes of wound healing and tissue repair. These results also demonstrate the significance of using peptides as an important tool for the discovery of simple and novel drug scaffolds.

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Peptídeos cíclicos de biomassa vegetal: características, diversidade, biossíntese e atividades biológicas

Cited by 12 publications

References 83 publications

Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles

A new peptide from Jatropha curcas seeds: Unusual sequence and insights into its synthetic analogue that enhances proteolytic activity of papain

Linear Peptide Analogues from Jatropha’s Orbitides Promote Migration of Human Neonatal Foreskin Fibroblasts in vitro and Collagen Deposition

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