Cryptides: latent peptides everywhere

Iavarone, Federica; Desiderio, Claudia; Vitali, Alberto; Messana, Irene; Martelli, Claudia; Castagnola, Massimo; Cabras, Tiziana

doi:10.1080/10409238.2018.1447543

Cited by 43 publications

(34 citation statements)

References 157 publications

(175 reference statements)

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“…The combination of the overall resulting data provided a comprehensive characterization of EP tumor tissue proteome matching the challenging features and balancing the pitfalls of both analytical approaches. Top-down proteomics typically profiles small proteins and peptides, including the challenging identification of naturally occurring bioactive protein fragments, the so-called "cryptic peptides" [17] of relevance in clinical proteomic studies. This approach, by manual inspection of the MS/MS spectra and de novo sequencing, can precisely identify and localize PTMs along the sequence, which are interesting to investigate with respect to the diverse tumor locations and the grade of aggressiveness.…”

Section: Resultsmentioning

confidence: 99%

Ependymoma Pediatric Brain Tumor Protein Fingerprinting by Integrated Mass Spectrometry Platforms: A Pilot Investigation

Rossetti

Massimi

Martelli

et al. 2020

Cancers

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Ependymoma pediatric brain tumor occurs at approximate frequencies of 10-15% in supratentorial and 20-30% in posterior fossa regions. These tumors have an almost selective response to surgery and relative and confirmed resistance to radiotherapy and chemotherapic agents, respectively. Alongside histopathological grading, clinical and treatment evaluation of ependymomas currently consider the tumor localization and the genomic outlined associated molecular subgroups, with the supratentorial and the posterior fossa ependymomas nowadays considered diverse diseases. On these grounds and in trying to better understand the molecular features of these tumors, the present investigation aimed to originally investigate the proteomic profile of pediatric ependymoma tissues of different grade and localization by mass spectrometry platforms to disclose potential distinct protein phenotypes. To this purpose, acid-soluble and acid-insoluble fractions of ependymoma tumor tissues homogenates were analyzed by LC-MS following both the top-down and the shotgun proteomic approaches, respectively, to either investigate the intact proteome or its digested form. The two approaches were complementary in profiling the ependymoma tumor tissues and showed distinguished profiles for supratentorial and posterior fossa ependymomas and for WHO II and III tumor grades. Top-down proteomic analysis revealed statistically significant higher levels of thymosin beta 4, 10 kDa heat shock protein, non-histone chromosomal protein HMG-17, and mono-/uncitrullinated forms ratio of the glial fibrillary acidic protein (GFAP) fragment 388-432 in supratentorial ependymomas-the same GFAP fragment as well as the hemoglobin alpha-and the beta-chain marked grade II with respect to grade III posterior fossa ependymomas. Gene ontology classification of shotgun data of the identified cancer and the non-cancer related proteins disclosed protein elements exclusively marking tumor localization and pathways that were selectively overrepresented. These results, although preliminary, seem consistent with different protein profiles of ependymomas of diverse grade of aggressiveness and brain region development and contributed to enlarging the molecular knowledge of this still enigmatic tumor.

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Section: Resultsmentioning

confidence: 99%

Ependymoma Pediatric Brain Tumor Protein Fingerprinting by Integrated Mass Spectrometry Platforms: A Pilot Investigation

Rossetti

Massimi

Martelli

et al. 2020

Cancers

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“…In this scenario, increasing interest has arisen for AMPs, a large group of natural molecules present in all micro- and macro-organisms, as an essential part of their own defenses, and for cryptides, known to derive from physiological proteins [4, 5, 9, 10, 30]. The most intriguing peculiarity of these molecules is the wide-spectrum antimicrobial activity, achieved by a direct action against microbial targets or indirectly, via activation of host immune responses [31].…”

Section: Discussionmentioning

confidence: 99%

Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins

et al. 2018

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Background/Aims: New antivirals are needed to supplement or replace currently used drugs. The aim of this study was to evaluate the antiviral activity of synthetic peptides derived from physiological proteins. Methods: Vero cell monolayers were infected with herpes simplex virus 1, vesicular stomatitis virus, adenovirus, and coxsackievirus B5 strains in the presence of different concentrations of the selected peptides and viral yield was determined by plaque reduction assays to evaluate the antiviral activity of the peptides. Virucidal activity was evaluated by determining the residual infectivity of viral suspensions treated for 1 h with the peptides at the same concentrations as in the viral yield assays. Results: Among the investigated peptides, the killer peptide proved to exert a considerable antiviral activity against herpes simplex virus, attributable to a direct effect on virus particles, while its derivative K10S showed to be effective against the four investigated virus strains only at the highest concentration tested, yet, the inhibitory effects were only partial. Conclusion: Overall, initial evidence is provided on the antiviral activity of several peptides, as well as of their derivatives. Further investigation is warranted to ascertain the mechanism of action in order to develop new potential antiviral drugs.

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“…In recent years, different studies have focused on the biological activity of peptide fragments derived from precursor proteins. These latent peptides are called cryptides and can be derived from natural cleavage of proteins (for example, milk caseins degradation into peptides by LAB) or in vitro proteolysis (Iavarone et al 2018). Many natural cryptides have been shown to display antifungal activities, lactoferricin (Lfcin) being one of the most studied (Fernandes & Carter, 2017).…”

Section: Unnatural Peptidesmentioning

confidence: 99%

Natural Antifungal Peptides/Proteins as Model for Novel Food Preservatives

Thery

Lynch

Arendt

2019

Comp Rev Food Sci Food Safe

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A large range of ingredients for food and food products are subject to fungal contamination, which is a major cause of destruction of crops, exposure of animals and humans to invasive mycotoxins, and food spoilage. The resistance of fungal species to common preservation methods highlights the necessity of new ways to increase the shelf life of raw material for food and food products. Antimicrobial peptides and proteins (AMPs) are essential members of the immune system of most living organisms. Due to their broad range of activity and their stability to commonly used food processes, they represent promising alternatives to traditional preservatives. However, despite the growing number of reports of potential food applications of these AMPs, the number of approved peptides is low. Poor solubility, toxicity, and a time‐consuming extraction are hurdles that limit their application in food products. Thanks to a deep understanding of the key determinants of their activity, the development of optimized synthetic peptides has reduced these drawbacks. This review presents natural and synthetic antifungal peptides/proteins (AFPs), effective against food‐related fungi, with particular emphasis on AFPs from plant sources. The design of novel antifungal peptides via key elements of antifungal activity is also reviewed. The potential applications of natural and synthetic AFPs as novel antifungal food preservatives are finally discussed.

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Cryptides: latent peptides everywhere

Cited by 43 publications

References 157 publications

Ependymoma Pediatric Brain Tumor Protein Fingerprinting by Integrated Mass Spectrometry Platforms: A Pilot Investigation

Ependymoma Pediatric Brain Tumor Protein Fingerprinting by Integrated Mass Spectrometry Platforms: A Pilot Investigation

Antiviral Activity of Synthetic Peptides Derived from Physiological Proteins

Natural Antifungal Peptides/Proteins as Model for Novel Food Preservatives

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