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

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/24:00136705

Organizace

Přírodovědecká fakulta – Masarykova univerzita – Repozitář

DOI

https://doi.org/10.1093/nar/gkae420

UT WoS

001233323700001

EID Scopus

2-s2.0-85197771239

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.
Změněno: 5. 3. 2026 00:50, RNDr. Daniel Jakubík

Anotace

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 20:33