Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Pietro, Sormanni"'
Publikováno v:
Open Biology, Vol 14, Iss 5 (2024)
Most successes in computational protein engineering to date have focused on enhancing one biophysical trait, while multi-trait optimization remains a challenge. Different biophysical properties are often conflicting, as mutations that improve one ten
Externí odkaz:
https://doaj.org/article/8ffedd5c6a95449f880744967c3da0b7
Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids
Autor:
Marc Oeller, Ryan J. D. Kang, Hannah L. Bolt, Ana L. Gomes dos Santos, Annika Langborg Weinmann, Antonios Nikitidis, Pavol Zlatoidsky, Wu Su, Werngard Czechtizky, Leonardo De Maria, Pietro Sormanni, Michele Vendruscolo
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract Non-natural amino acids are increasingly used as building blocks in the development of peptide-based drugs as they expand the available chemical space to tailor function, half-life and other key properties. However, while the chemical space
Externí odkaz:
https://doaj.org/article/0caac934400240c99334cfb366d281f4
Publikováno v:
mAbs, Vol 15, Iss 1 (2023)
ABSTRACTAntibody drugs should exhibit not only high-binding affinity for their target antigens but also favorable physicochemical drug-like properties. Such drug-like biophysical properties are essential for the successful development of antibody dru
Externí odkaz:
https://doaj.org/article/375ca2578f7d4343a49f80dafa044d39
Autor:
Angelo Rosace, Anja Bennett, Marc Oeller, Mie M. Mortensen, Laila Sakhnini, Nikolai Lorenzen, Christian Poulsen, Pietro Sormanni
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Antibodies find key applications in research, diagnostics, and therapeutics, but their development can be impeded by poor stability or solubility. Here the authors developed a computational strategy that enables antibody optimisation, without affecti
Externí odkaz:
https://doaj.org/article/1130c0e57b5e4de4ab65ffe227965175
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Abstract The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations. High solubility is therefore a key requirement for the development of p
Externí odkaz:
https://doaj.org/article/b5f7828ff8824c158a7da76797f5c5ae
Autor:
Rahul Khetan, Robin Curtis, Charlotte M. Deane, Johannes Thorling Hadsund, Uddipan Kar, Konrad Krawczyk, Daisuke Kuroda, Sarah A. Robinson, Pietro Sormanni, Kouhei Tsumoto, Jim Warwicker, Andrew C.R. Martin
Publikováno v:
mAbs, Vol 14, Iss 1 (2022)
Therapeutic monoclonal antibodies and their derivatives are key components of clinical pipelines in the global biopharmaceutical industry. The availability of large datasets of antibody sequences, structures, and biophysical properties is increasingl
Externí odkaz:
https://doaj.org/article/c03a214cecc447edb4481e81ade59152
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/a821306fec904a68817a6650e8ed57be
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
Autor:
Suman De, David C. Wirthensohn, Patrick Flagmeier, Craig Hughes, Francesco A. Aprile, Francesco S. Ruggeri, Daniel R. Whiten, Derya Emin, Zengjie Xia, Juan A. Varela, Pietro Sormanni, Franziska Kundel, Tuomas P. J. Knowles, Christopher M. Dobson, Clare Bryant, Michele Vendruscolo, David Klenerman
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Amyloid beta (Aβ42) peptides form heterogeneous mixtures of aggregates, which are closely linked to Alzheimer’s disease. This study shows how different types of Aβ42 aggregates are associated with distinct mechanisms of toxicity
Externí odkaz:
https://doaj.org/article/dda94a3ed6064b0ba41892597f9160ae
Autor:
Michele Perni, Annemieke van der Goot, Ryan Limbocker, Tjakko J. van Ham, Francesco A. Aprile, Catherine K. Xu, Patrick Flagmeier, Karen Thijssen, Pietro Sormanni, Giuliana Fusco, Serene W. Chen, Pavan K. Challa, Julius B. Kirkegaard, Romain F. Laine, Kai Yu Ma, Martin B. D. Müller, Tessa Sinnige, Janet R. Kumita, Samuel I. A. Cohen, Renée Seinstra, Gabriele S. Kaminski Schierle, Clemens F. Kaminski, Denise Barbut, Alfonso De Simone, Tuomas P. J. Knowles, Michael Zasloff, Ellen A. A. Nollen, Michele Vendruscolo, Christopher M. Dobson
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
The aggregation of α-synuclein is a hallmark of Parkinson's disease (PD) and a variety of related neurological disorders. A number of mutations in this protein, including A30P and A53T, are associated with familial forms of the disease. Patients car
Externí odkaz:
https://doaj.org/article/40381e7ca771461e9f79bf4da8952019
Publikováno v:
Frontiers in Neuroscience, Vol 15 (2021)
There is great interest in drug discovery programs targeted at the aggregation of the 42-residue form of the amyloid β peptide (Aβ42), since this molecular process is closely associated with Alzheimer’s disease. The use of bicyclic peptides may o
Externí odkaz:
https://doaj.org/article/2f790f153299457a8d1ab6d497bc89c5