{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo Q"],"funding":["National Research Foundation Singapore (National Research Foundation-Prime Minister's office, Republic of Singapore)","Ministry of Education - Singapore (MOE)","National Research Foundation Singapore","Ministry of Education - Singapore"],"pagination":["5771"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9526746"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Marine mussels achieve strong underwater adhesion by depositing mussel foot proteins (Mfps) that form coacervates during the protein secretion. However, the molecular mechanisms that govern the phase separation behaviors of the Mfps are still not fully understood. Here, we report that GK-16*, a peptide derived from the primary adhesive protein Mfp-5, forms coacervate in seawater conditions. Molecular dynamics simulations combined with point mutation experiments demonstrate that Dopa- and Gly- mediated hydrogen-bonding interactions are essential in the coacervation process. The properties of GK-16* coacervates could be controlled by tuning the strength of the electrostatic and Dopa-mediated hydrogen bond interactions via controlling the pH and salt concentration of the solution. The GK-16* "],"journal":["Nature communications"],"pubmed_title":["Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides."],"pmcid":["PMC9526746"],"funding_grant_id":["MOE-T2EP30220-0006","NRF-NRFF11-2019-0004"],"pubmed_authors":["Qian X","Gao H","Chen S","Yu J","Guo Q","Zou G"],"additional_accession":[]},"is_claimable":false,"name":"Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides.","description":"Marine mussels achieve strong underwater adhesion by depositing mussel foot proteins (Mfps) that form coacervates during the protein secretion. However, the molecular mechanisms that govern the phase separation behaviors of the Mfps are still not fully understood. Here, we report that GK-16*, a peptide derived from the primary adhesive protein Mfp-5, forms coacervate in seawater conditions. Molecular dynamics simulations combined with point mutation experiments demonstrate that Dopa- and Gly- mediated hydrogen-bonding interactions are essential in the coacervation process. The properties of GK-16* coacervates could be controlled by tuning the strength of the electrostatic and Dopa-mediated hydrogen bond interactions via controlling the pH and salt concentration of the solution. The GK-16* ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-22T03:33:16.707Z","creation":"2025-02-19T00:23:29.649Z"},"accession":"S-EPMC9526746","cross_references":{"pubmed":["36182948"],"doi":["10.1038/s41467-022-33545-w"]}}