Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Michele Larocca"'
In this study, we addressed an important drawback of our previously reported tetraplatinated (metallo)porphyrin-based photosensitizers (PSs) for photodynamic therapy (PDT), namely, the poor solubility in aqueous media. We aimed to create tetraplatina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0ffc23b52470a7ebb529608b845a0e4
https://www.zora.uzh.ch/id/eprint/205160/
https://www.zora.uzh.ch/id/eprint/205160/
Autor:
Lukas Schneider, Ekaterina Slyshkina, Vipin Babu, Bernhard Spingler, Michele Larocca, Christiane König, Roxane Padrutt, Wenyu Wu, Stefano Ferrari
Publikováno v:
Photochemical & Photobiological Sciences. 18:2792-2803
We report the first exocyclically metallated tetrapyridinoporphyrazine, [tetrakis-(trans-Pt(NH3)2Cl)-tetra(3,4-pyrido)porphyrazine-zinc(II)](NO3)4 (4), synthesized in a multistep synthesis starting from 3,4-pyridinedicarbonitrile (1). The synthetic p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4b380f0b000b66fe71b352d10d3b8ea
https://doi.org/10.1039/c9pp00336c
https://doi.org/10.1039/c9pp00336c
Publikováno v:
Larocca, M, Foglia, F & Cilibrizzi, A 2019, ' Dihedral Angle Calculations to Elucidate the Folding of Peptides through Its Main Mechanical Forces ', Biochemistry, vol. 58, no. 8, pp. 1032-1037 . https://doi.org/10.1021/acs.biochem.8b01101
This study reports a general method to calculate dihedral angles (φ and ψ) of a given amino acid sequence, focusing on potential energy and torque moment concepts. By defining these physical measures in relation to the chemical interactions that oc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b3829a9ff14666d62c3587fa0989280
https://doi.org/10.1021/acs.biochem.8b01101
https://doi.org/10.1021/acs.biochem.8b01101
Autor:
Michele Larocca
Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5182ca693ba3274552af8e0b11d5c96b
https://doi.org/10.26434/chemrxiv.12000132.v2
https://doi.org/10.26434/chemrxiv.12000132.v2
Autor:
Michele Larocca
Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f941a54091f03dd63a641a804bb24e08
https://doi.org/10.26434/chemrxiv.12000132.v1
https://doi.org/10.26434/chemrxiv.12000132.v1
Autor:
Riccardo Rubbiani, Wenyu Wu, Lukas Schneider, Doris Hinger, Vipin Babu, Anu Naik, Bernhard Spingler, Michele Larocca, Christiane König, Gilles Gasser, Roxane Padrutt, Caroline Maake, Stefano Ferrari
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2020, ⟨10.1039/D0CC05196A⟩
Chemical Communications, Royal Society of Chemistry, 2020, ⟨10.1039/D0CC05196A⟩
We report the synthesis of novel tetraplatinated metalloporphyrin-based photosensitizers (PSs) for photodynamic therapy (PDT), their characterization, cellular uptake and localization, as well as the determination of their in vitro light-induced anti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b54e88f860424e84bf4b9dd3e7c30aa4
https://hal.archives-ouvertes.fr/hal-02973034/document
https://hal.archives-ouvertes.fr/hal-02973034/document
Publikováno v:
Journal of Molecular Structure. 1229:129802
The folding process has been described as the output of main mechanical forces which generate from the specific chemical interplay among residues of an amino acid chain. Recently, we have reported that dihedral angle values in (poly)peptides can be c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f346c817babd397797aaecdf736690a5
https://doi.org/10.1016/j.molstruc.2020.129802
https://doi.org/10.1016/j.molstruc.2020.129802
Autor:
Nicola Castellucci, Elena Maria Ghibaudi, Michele Larocca, Andrea Cornia, Matteo Calvaresi, Mattia Tedesco, Lorenzo Milli, Claudia Tomasini, Francesco Zerbetto
Two epimeric series of foldamers characterized by the presence of a repeating alpha-epsilon-dipeptide unit have been prepared and characterized by 1H NMR and ECD spectroscopies together with X-ray diffraction. The first series contains L-Ala and D-4-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26a300bb29b05d8c81d2517ea7c50c20
http://hdl.handle.net/2318/151897
http://hdl.handle.net/2318/151897