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  1. Article ; Online: Probing the Importance of the G-Quadruplex Grooves for the Activity of the Anti-HIV-Integrase Aptamer T30923

    Veronica Esposito / Francesca Esposito / Antonietta Pepe / Isabel Gomez Monterrey / Enzo Tramontano / Luciano Mayol / Antonella Virgilio / Aldo Galeone

    International Journal of Molecular Sciences, Vol 21, Iss 5637, p

    2020  Volume 5637

    Abstract: In this paper, we report studies concerning four variants of the G-quadruplex forming anti-HIV-integrase aptamer T30923, in which specific 2′-deoxyguanosines have been singly replaced by 8-methyl-2′-deoxyguanosine residues, with the aim to exploit the ... ...

    Abstract In this paper, we report studies concerning four variants of the G-quadruplex forming anti-HIV-integrase aptamer T30923, in which specific 2′-deoxyguanosines have been singly replaced by 8-methyl-2′-deoxyguanosine residues, with the aim to exploit the methyl group positioned in the G-quadruplex grooves as a steric probe to investigate the interaction aptamer/target. Although, the various modified aptamers differ in the localization of the methyl group, NMR, circular dichroism (CD), electrophoretic and molecular modeling data suggest that all of them preserve the ability to fold in a stable dimeric parallel G-quadruplex complex resembling that of their natural counterpart T30923. However, the biological data have shown that the T30923 variants are characterized by different efficiencies in inhibiting the HIV-integrase, thus suggesting the involvement of the G-quadruplex grooves in the aptamer/target interaction.
    Keywords G-quadruplex ; 8-methyl-2′-deoxyguanosine ; aptamers ; integrase ; HIV ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2020-08-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides

    Federica Boraldi / Pasquale Moscarelli / Brigida Bochicchio / Antonietta Pepe / Anna M. Salvi / Daniela Quaglino

    Scientific Reports, Vol 8, Iss 1, Pp 1-

    2018  Volume 11

    Abstract: Abstract Heparan sulfates (HSs) modulate tissue elasticity in physiopathological conditions by interacting with various matrix constituents as tropoelastin and elastin-derived peptides. HSs bind also to protein moieties accelerating amyloid formation and ...

    Abstract Abstract Heparan sulfates (HSs) modulate tissue elasticity in physiopathological conditions by interacting with various matrix constituents as tropoelastin and elastin-derived peptides. HSs bind also to protein moieties accelerating amyloid formation and influencing cytotoxic properties of insoluble fibrils. Interestingly, amyloidogenic polypeptides, despite their supposed pathogenic role, have been recently explored as promising bio-nanomaterials due to their unique and interesting properties. Therefore, we investigated the interactions of HSs, obtained from different sources and exhibiting various degree of sulfation, with synthetic amyloidogenic elastin-like peptides (ELPs), also looking at the effects of these interactions on cell viability and cell behavior using in vitro cultured fibroblasts, as a prototype of mesenchymal cells known to modulate the soft connective tissue environment. Results demonstrate, for the first time, that HSs, with differences depending on their sulfation pattern and chain length, interact with ELPs accelerating aggregation kinetics and amyloid-like fibril formation as well as self-association. Furthermore, these fibrils do not negatively affect fibroblasts’ cell growth and parameters of redox balance, and influence cellular adhesion properties. Data provide information for a better understanding of the interactions altering the elastic component in aging and in pathologic conditions and may pave the way for the development of composite matrix-based biomaterials.
    Keywords Medicine ; R ; Science ; Q
    Subject code 612
    Language English
    Publishing date 2018-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Non-invasive characterization of hybrid gelatin:poly-l-lactide electrospun scaffolds using second harmonic generation and multiphoton imaging

    Piccirillo, Germano / Mauro V. Ditaranto / Nora F.S. Feuerer / Daniel A. Carvajal Berrio / Eva M. Brauchle / Antonietta Pepe / Brigida Bochicchio / Katja Schenke-Layland / Svenja Hinderer

    Journal of materials chemistry. 2018 Oct. 17, v. 6, no. 40

    2018  

    Abstract: Hybrid scaffolds composed of synthetic polymers and naturally occurring components have become more relevant in the field of tissue engineering and regenerative medicine. Synthetic polymers are responsible for scaffold durability, strength and structural ...

    Abstract Hybrid scaffolds composed of synthetic polymers and naturally occurring components have become more relevant in the field of tissue engineering and regenerative medicine. Synthetic polymers are responsible for scaffold durability, strength and structural integrity; however, often do not provide biological signals. Introducing a biological component leads to more advanced and biocompatible scaffolds. In order to use these scaffolds as implants, a deeper knowledge of material characteristics and the impact of the biological component on the scaffold mechanical properties are required. Furthermore, it is necessary to implement fast, easy and non-invasive methods to determine material characteristics. In this work, we aimed to generate gelatin-poly-l-lactide (PLA) hybrids via electrospinning with defined, controllable and tunable scaffold characteristics. Using Raman microspectroscopy, we demonstrated the effectiveness of the cross-linking reaction and evaluated the increasing PLA content in the hybrid scaffolds with a non-invasive approach. Using multiphoton microscopy, we showed that gelatin fibers electrospun from a fluorinated solvent exhibit a second harmonic generation (SHG) signal typical for collagen-like structures. Compared to pure gelatin, where the SHG signal vanishes after cross-linking, the signal could be preserved in the hybrid scaffolds even after cross-linking. Furthermore, we non-invasively imaged cellular growth of human dermal fibroblasts on the hybrid electrospun scaffolds and performed fluorescence lifetime imaging microscopy on the cell-seeded hybrids, where we were able to discriminate between cells and scaffolds. Here, we successfully employed non-invasive methods to evaluate scaffold characteristics and investigate cell–material interactions.
    Keywords Raman spectroscopy ; cell growth ; crosslinking ; durability ; fibroblasts ; fluorescence microscopy ; gelatin ; humans ; image analysis ; mechanical properties ; medicine ; polymers ; solvents ; tissue engineering
    Language English
    Dates of publication 2018-1017
    Size p. 6399-6412.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 2702241-9
    ISSN 2050-7518 ; 2050-750X
    ISSN (online) 2050-7518
    ISSN 2050-750X
    DOI 10.1039/c8tb02026d
    Database NAL-Catalogue (AGRICOLA)

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  4. Article: Interactions between elastin-like peptides and an insulating poly(ortho-aminophenol) membrane investigated by AFM and XPS

    Carbone, Maria Elvira / Anna Maria Salvi / Antonietta Pepe / Antonio Guerrieri / Brigida Bochicchio / Daniela Quaglino / Federica Boraldi / Giuliana Bianco / Pasquale Moscarelli / Rosanna Ciriello

    Analytical and bioanalytical chemistry. 2018 Aug., v. 410, no. 20

    2018  

    Abstract: This investigation was undertaken to explore the mutual recognition of the pentapeptide (ValGlyGlyValGly)n, a hydrophobic elastin-like peptide (ELP), suspended in deionized water in monomer (n = 1) and trimer (n = 3) forms and the outer surface of a very ...

    Abstract This investigation was undertaken to explore the mutual recognition of the pentapeptide (ValGlyGlyValGly)n, a hydrophobic elastin-like peptide (ELP), suspended in deionized water in monomer (n = 1) and trimer (n = 3) forms and the outer surface of a very thin, insulating polymer, poly(ortho-aminophenol) (PoAP), electrochemically grown on a platinum foil by cyclic voltammetry in a neutral medium (phosphate-buffered saline, I = 0.1M) immersed in the suspension. As a prior task, the proved propensity of the ValGlyGlyValGly sequence, at the given minimal length (three or more repeats), to self-assemble into amyloid-like fibrils when solubilized in an aqueous environment was considered within the framework of testing PoAP surfaces for the specific detection of amyloid precursors. From our knowledge of the chemical structure and physical properties of both biomacromolecule families obtained in previous studies, we focused on the efficacy of the binding sites offered to ELP fibrils by PoAP in its as-prepared form or properly modified either by postsynthesis oxidation or by adsorption/entrapping of ELP monomer(s) with or without protecting terminal groups. Consistent with all methods of preparation, the best surfaces, recognizable by the trimer fibrils, are those modified to carry a larger number of carbonyls, particularly by entrapment of ELP monomer(s) during PoAP electrosynthesis using an imprinting-inspired method. The degree of attachment of fibrillar aggregates, detected by atomic force microscopy and X-ray photoelectron spectroscopy, provides unequivocal evidence of the cooperative forces involving PoAP–ELP interactions. The results obtained suggest the prospect of using the proposed Pt/PoAP/ELP systems as biodetectors in Alzheimer disease. Graphical abstract Synthesis steps of Pt/PoAP/ELP electrodes for amyloid detection. AFM = Atomic Force Microscopy, CV = Cyclic Voltammetry, ELPs = Elastin like Peptides, PoAP = Poly ortho-Aminophenol, Pt = Platinum, XPS = X-ray Photoelectron Spectroscopy
    Keywords adsorption ; Alzheimer disease ; amyloid ; atomic force microscopy ; binding sites ; elastin ; electrochemistry ; electrodes ; electrosynthesis ; foil ; hydrophobicity ; oxidation ; peptides ; physical properties ; platinum ; polymers ; solubilization ; X-ray photoelectron spectroscopy
    Language English
    Dates of publication 2018-08
    Size p. 4925-4941.
    Publishing place Springer Berlin Heidelberg
    Document type Article
    ISSN 1618-2642
    DOI 10.1007/s00216-018-1142-3
    Database NAL-Catalogue (AGRICOLA)

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