biostudies-literatureTolmachev DAAcademy of FinlandNovo NordiskFinnCERES Materials Bioeconomy EcosystemNovo Nordisk Fonden5638-5653https://www.ebi.ac.uk/biostudies/studies/S-EPMC10716855biostudies-literatureUnknown24(12)Future sustainable materials based on designer biomolecules require control of the solution assembly, but also interfacial interactions. Alcohol treatments of protein materials are an accessible means to this, making understanding of the process at the molecular level of seminal importance. We focus here on the influence of ethanol on spidroins, the main proteins of silk. By large-scale atomistically detailed molecular dynamics (MD) simulations and interconnected experiments, we characterize the protein aggregation, secondary structure changes, molecular level origins of them, and solvation environment changes for the proteins, as induced by ethanol as a solvation additive. The MD and circular dichoroism (CD) findings jointly show that ethanol promotes ordered structure in the protein moleBiomacromoleculesSpidroins under the Influence of Alcohol: Effect of Ethanol on Secondary Structure and Molecular Level Solvation of Silk-Like Proteins.PMC10716855346111NNF20OC0061306NNF22OC0074060346105Malkamaki MLinder MBSammalkorpi MTolmachev DAfalseSpidroins under the Influence of Alcohol: Effect of Ethanol on Secondary Structure and Molecular Level Solvation of Silk-Like Proteins.Future sustainable materials based on designer biomolecules require control of the solution assembly, but also interfacial interactions. Alcohol treatments of protein materials are an accessible means to this, making understanding of the process at the molecular level of seminal importance. We focus here on the influence of ethanol on spidroins, the main proteins of silk. By large-scale atomistically detailed molecular dynamics (MD) simulations and interconnected experiments, we characterize the protein aggregation, secondary structure changes, molecular level origins of them, and solvation environment changes for the proteins, as induced by ethanol as a solvation additive. The MD and circular dichoroism (CD) findings jointly show that ethanol promotes ordered structure in the protein mole2023-01-01T00:00:00Z2023 Dec2026-05-28T13:02:56.635Z2025-04-04T21:20:28.522ZS-EPMC107168553801957710.1021/acs.biomac.3c00637