Elucidating ATP’s role as solubilizer of biomolecular aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

et al.

eLife, Journal Year: 2024, Volume and Issue: 13

Published: Oct. 30, 2024

Proteins occurring in significantly high concentrations cellular environments (over 100 mg/ml) and functioning crowded cytoplasm, often face the prodigious challenges of aggregation which are pathological hallmark aging critically responsible for a wide spectrum rising human diseases. Here, we combine joint-venture complementary wet-lab experiment molecular simulation to discern potential ability adenosine triphosphate (ATP) as solubilizer protein aggregates. We show that ATP prevents both condensation aggregation-prone intrinsically disordered Aβ40 promotes dissolution preformed Computer links ATP’s solubilizing role its modulate protein’s structural plasticity by unwinding conformation. is positioned superior biological aggregates over traditional chemical hydrotropes, potentially holding promises therapeutic interventions protein-aggregation-related Going beyond conventional activity energy currency, amphiphilic nature enables protein-specific interaction would enhance efficiency processes.

Language: Английский

Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

et al.

eLife, Journal Year: 2024, Volume and Issue: 13

Published: July 10, 2024

Proteins occurring in significantly high concentrations cellular environments (over 100 mg/ml) and functioning crowded cytoplasm, often face the prodigious challenges of aggregation which are pathological hallmark aging critically responsible for a wide spectrum rising human diseases. Here, we combine joint-venture complementary wet-lab experiment molecular simulation to discern potential ability adenosine triphosphate (ATP) as solubilizer protein aggregates. We show that ATP prevents both condensation aggregation-prone intrinsically disordered Aβ40 promotes dissolution preformed Computer links ATP’s solubilizing role its modulate protein’s structural plasticity by unwinding conformation. is positioned superior biological aggregates over traditional chemical hydrotropes, potentially holding promises therapeutic interventions protein-aggregation-related Going beyond conventional activity energy currency, amphiphilic nature enables protein-specific interaction would enhance efficiency processes.

Language: Английский

Citations

3
Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Open Access

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

et al.

Published: Sept. 24, 2024

Proteins occurring in significantly high concentrations cellular environments (over 100 mg/mL) and functioning crowded cytoplasm, often face the prodigious challenges of aggregation which are pathological hallmark aging critically responsible for a wide spectrum rising human diseases. Here we combine joint-venture complementary wet-lab experiment molecular simulation to discern potential ability adenosine triphosphate (ATP) as solubilizer protein aggregates. We show that ATP prevents both condensation aggregation-prone intrinsically disordered Aβ40 promotes dissolution pre-formed Computer links ATP’s solubilizing role its modulate protein’s structural plasticity by unwinding conformation. is positioned superior biological aggregates over traditional chemical hydrotropes, potentially holding promises therapeutic interventions protein-aggregation related Going beyond conventional activity energy currency, amphiphilic nature enables protein-specific interaction would enhance efficiency processes.

Language: Английский

Citations

3
Elucidating ATP’s Role as Solubilizer of Biomolecular Aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Jan. 16, 2024

Abstract Proteins occurring in significantly high concentrations cellular environments (over 100 mg/mL) and functioning crowded cytoplasm, often face the prodigious challenges of aggregation which are pathological hallmark aging critically responsible for a wide spectrum rising human diseases. Here we combine joint-venture complementary wet-lab experiment molecular simulation to discern potential ability adenosine triphosphate (ATP) as solubilizer protein aggregates. We show that ATP prevents both condensation aggregation-prone intrinsically disordered Aβ40 promotes dissolution pre-formed Computer links ATP’s solubilizing role its modulate protein’s structural plasticity by unwinding conformation. is positioned superior biological aggregates over traditional chemical hydrotropes, potentially holding promises therapeutic interventions protein-aggregation related Going beyond conventional activity energy currency, amphiphilic nature enables protein-specific interaction would enhance efficiency processes.

Language: Английский

Citations

1
Elucidating ATP’s role as solubilizer of biomolecular aggregate DOI Creative Commons

Susmita Sarkar,

Saurabh Gupta,

Chiranjit Mahato

et al.

eLife, Journal Year: 2024, Volume and Issue: 13

Published: Oct. 30, 2024

Proteins occurring in significantly high concentrations cellular environments (over 100 mg/ml) and functioning crowded cytoplasm, often face the prodigious challenges of aggregation which are pathological hallmark aging critically responsible for a wide spectrum rising human diseases. Here, we combine joint-venture complementary wet-lab experiment molecular simulation to discern potential ability adenosine triphosphate (ATP) as solubilizer protein aggregates. We show that ATP prevents both condensation aggregation-prone intrinsically disordered Aβ40 promotes dissolution preformed Computer links ATP’s solubilizing role its modulate protein’s structural plasticity by unwinding conformation. is positioned superior biological aggregates over traditional chemical hydrotropes, potentially holding promises therapeutic interventions protein-aggregation-related Going beyond conventional activity energy currency, amphiphilic nature enables protein-specific interaction would enhance efficiency processes.

Language: Английский

Citations

0