Insecticidal diversity of butterfly pea (Clitoria ternatea) accessions

Oguis, Georgianna Kae; Gilding, Edward K.; Huang, Yen‐Hua; Poth, Aaron G.; Jackson, Mark A.; Craik, David J.

doi:10.1016/j.indcrop.2020.112214

Cited by 18 publications

(15 citation statements)

References 19 publications

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“…Molecular stability represents a crucial requirement for AMPs to be used as new active pharmaceutical ingredients. Several disulfide-rich peptide families, such as plant cyclotides [ 208 ] or primate-related θ-defensin [ 209 ] display Cys-stabilized structures with a well-defined three-dimensional motif. Focusing on AMP modifications, it is possible to realize the cyclization by three main post-translational methods, i.e.…”

Section: Stability Improvements Of Peptides Against Proteolytic Susceptibilitymentioning

confidence: 99%

Insect antimicrobial peptides: potential weapons to counteract the antibiotic resistance

Manniello

Moretta

Salvia

et al. 2021

Cell. Mol. Life Sci.

156

111

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Misuse and overuse of antibiotics have contributed in the last decades to a phenomenon known as antibiotic resistance which is currently considered one of the principal threats to global public health by the World Health Organization. The aim to find alternative drugs has been demonstrated as a real challenge. Thanks to their biodiversity, insects represent the largest class of organisms in the animal kingdom. The humoral immune response includes the production of antimicrobial peptides (AMPs) that are released into the insect hemolymph after microbial infection. In this review, we have focused on insect immune responses, particularly on AMP characteristics, their mechanism of action and applications, especially in the biomedical field. Furthermore, we discuss the Toll, Imd, and JAK-STAT pathways that activate genes encoding for the expression of AMPs. Moreover, we focused on strategies to improve insect peptides stability against proteolytic susceptibility such as D-amino acid substitutions, N-terminus modification, cyclization and dimerization.

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Section: Stability Improvements Of Peptides Against Proteolytic Susceptibilitymentioning

confidence: 99%

Insect antimicrobial peptides: potential weapons to counteract the antibiotic resistance

Manniello

Moretta

Salvia

et al. 2021

Cell. Mol. Life Sci.

156

111

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“…Based on reported data, generally C. ternatea root extracts seem to contain more potent anthelmintic components [29,30,31]. It is important to mention here that these cyclic peptides have been used recently to develop eco-friendly pesticide known as Sero-X® [32].…”

Section: Antimicrobial Propertiesmentioning

confidence: 98%

Clitoria ternatea - Shifting Paradigms: From Laboratory to Industry

Ranaweera

Chandana

2021

SAJRM

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Clitoria ternatea commonly known as Butterfly pea is a standard Ayurvedic medicinal plant used in many parts of south Asian countries. Traditional medicinal plants are a great alternative to find new treatments and for the development of novel antimicrobials to combat many diseases. In Ayurveda and traditional and folk medicine in several countries, decoction and extracts made from C. ternatea are recommended to be used for various medical treatments. C. ternatea extracts claimed to possess antibacterial, antiviral, and antifungal properties, which had been supported and validated by many in vitro and in vivo experiments. However, biologically active compound/s isolation and development novel compounds still remain in its infancy. Despite its enormous potential health benefits, only a single commercial product managed to reach industrial level production. C. ternatea cyclotide studies are also limited despite the fact that it the fastest known natural ligase discovered to date. These cyclotides are rapid peptide ligators and has been the focus of many recent studies on peptide ligation and cyclization for biotechnological applications. In this mini summary we have tried to point out innate unique biological properties of C. ternatea and suggested few future studies, more specifically on C. ternatea cyclotides development against bacterial heat shock proteins (Hsp 100) for novel antimicrobial discovery and development.

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“…While the y 20 2 + ion was not detectable, the observation of the b 9 ion (m/z = 1056.45) confirms cleavage at V9-P10 bond (Figure S3). The observation of intense internal fragment ions corresponding to the segments [10][11][12][13][14][15][16] (m/z = 893.29) and [17][18][19][20][21][22][23][24] (m/z = 914.46) establish that the three X-Pro bond cleavages dominate the fragmentation pattern of this cyclotide sequence. ctr pep 30: Of the 110 unique cyclotide sequences currently known from C. ternatea, 26 were detected in our previously reported transcriptomic analysis.…”

Section: Ms Fragmentation-based Classification Of Cyclotidesmentioning

confidence: 99%

“…[2,12,13] This has led to the recent release of an ecofriendly pesticide -SeroX®, made from Clitoria ternatea extracts and marketed in Australia. [14] Growing interest in cyclotide research has led to their identification from a variety of plant families such as Rubiaceae, Violaceae, Cucurbitaceae, Fabaceae and Solanaceae. [11,[15][16][17][18] Cyclotide sequences and structures can be divided mainly into three subfamilies: Möbius, Bracelet and trypsin-inhibitor subfamilies [19] (Figure 1A).…”

Section: Introductionmentioning

confidence: 99%

Mass Spectrometric Analysis of Cyclotides from Clitoria ternatea: Xxx‐Pro Bond Fragmentation as Convenient Diagnostic of Pro Residue Positioning

Kalmankar

Balaram

Venkatesan

2021

Chemistry An Asian Journal

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Cyclotides, a class of macrocyclic plant peptides, characterized by a cyclic backbone and three inter-locking disulfide bonds, may be divided into two major structural subfamilies, Möbius and Bracelet, based on the presence or absence of a specific proline residue. The present study describes the suite of cyclotides obtained from Clitoria ternatea, characterized by LCÀ MS and MS/MS techniques. Notable variations in product ion distributions were observed in cyclotides belonging to different structural subfamilies based on the number and positions of proline residues. For instance, Cter M which is an abundant Möbius cyclotide in this plant containing three proline residues, displayed distinct b-and y-ion characteristics in the MS/MS spectra compared to Cliotide T1, another commonly identified cyclotide but belonging to the Bracelet subfamily having two proline residues. The distinct fragmentation pattern of prototypical cyclotides of each structural subfamily, determined by Xxx-Pro bond fragmentation, was used to rapidly identify and sequence a novel cyclotide ctr pep 30 from this plant.

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Insecticidal diversity of butterfly pea (Clitoria ternatea) accessions

Cited by 18 publications

References 19 publications

Insect antimicrobial peptides: potential weapons to counteract the antibiotic resistance

Insect antimicrobial peptides: potential weapons to counteract the antibiotic resistance

Clitoria ternatea - Shifting Paradigms: From Laboratory to Industry

Mass Spectrometric Analysis of Cyclotides from Clitoria ternatea: Xxx‐Pro Bond Fragmentation as Convenient Diagnostic of Pro Residue Positioning

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