J
2024
AggreProt: a web server for predicting and engineering aggregation prone regions in proteins
PLANAS IGLESIAS, Joan; Simeon BORKO; Jan SWIATKOWSKI; Matej ELIAS; Martin HAVLÁSEK et al.
Základní údaje
Originální název
AggreProt: a web server for predicting and engineering aggregation prone regions in proteins
Autoři
PLANAS IGLESIAS, Joan; Simeon BORKO; Jan SWIATKOWSKI; Matej ELIAS; Martin HAVLÁSEK; Ondrej SALAMON; Ekaterina GRAKOVA; Antonín KUNKA; Tomas MARTINOVIC; Jiří DAMBORSKÝ; Jan MARTINOVIC a David BEDNÁŘ
Vydání
Nucleic Acids Research, Oxford, Oxford University Press, 2024, 0305-1048
Další údaje
Typ výsledku
Článek v odborném periodiku
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/24:00136705
Organizace
Přírodovědecká fakulta – Masarykova univerzita – Repozitář
Klíčová slova anglicky
SECONDARY STRUCTURE; BETA; DATABASE; DESIGN
Návaznosti
EF17_043/0009632, projekt VaV. LM2018140, projekt VaV. LM2023055, projekt VaV. LM2023069, projekt VaV. LX22NPO5107, projekt VaV. 857560, interní kód Repo. e-INFRA CZ II, velká výzkumná infrastruktura.
V originále
Recombinant proteins play pivotal roles in numerous applications including industrial biocatalysts or therapeutics. Despite the recent progress in computational protein structure prediction, protein solubility and reduced aggregation propensity remain challenging attributes to design. Identification of aggregation-prone regions is essential for understanding misfolding diseases or designing efficient protein-based technologies, and as such has a great socio-economic impact. Here, we introduce AggreProt, a user-friendly webserver that automatically exploits an ensemble of deep neural networks to predict aggregation-prone regions (APRs) in protein sequences. Trained on experimentally evaluated hexapeptides, AggreProt compares to or outperforms state-of-the-art algorithms on two independent benchmark datasets. The server provides per-residue aggregation profiles along with information on solvent accessibility and transmembrane propensity within an intuitive interface with interactive sequence and structure viewers for comprehensive analysis. We demonstrate AggreProt efficacy in predicting differential aggregation behaviours in proteins on several use cases, which emphasize its potential for guiding protein engineering strategies towards decreased aggregation propensity and improved solubility. The webserver is freely available and accessible at https://loschmidt.chemi.muni.cz/aggreprot/.
Zobrazeno: 4. 5. 2026 18:29