{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kurgan KW"],"funding":["NCRR NIH HHS","NHLBI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1108-1119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8044043"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["60(14)"],"pubmed_abstract":["Methods for maintaining membrane proteins in their native state after removal from the lipid bilayer are essential for the study of this important class of biomacromolecules. Common solubilization strategies range from the use of detergents to more complex systems that involve a polypeptide working in concert with lipids or detergents, such as nanodiscs, picodiscs, and peptidiscs, in which an engineered protein or synthetic peptide surrounds the membrane protein along with a lipid sheath. Picodiscs employ the protein saposin A, which naturally functions to facilitate lipid degradation in the lysozome. Saposin A-amphiphile complexes therefore tend to be most stable at acidic pH, which is not optimal for most membrane protein applications. In search of new picodisc assemblies, we have explor"],"journal":["Biochemistry"],"pubmed_title":["Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents."],"pmcid":["PMC8044043"],"funding_grant_id":["T32 HL007936","T32 HL110853","R01 GM125085","S10 RR023438","S10 RR028438","P41 RR002301","R01 GM117058","R01 GM061238","S10 RR029220","S10 RR025062","S10 RR008438","P41 GM103399","S10 RR002781"],"pubmed_authors":["Ge Y","Kurgan KW","Chen B","Brown KA","Ye X","Gellman SH","Falco Cobra P"],"additional_accession":[]},"is_claimable":false,"name":"Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.","description":"Methods for maintaining membrane proteins in their native state after removal from the lipid bilayer are essential for the study of this important class of biomacromolecules. Common solubilization strategies range from the use of detergents to more complex systems that involve a polypeptide working in concert with lipids or detergents, such as nanodiscs, picodiscs, and peptidiscs, in which an engineered protein or synthetic peptide surrounds the membrane protein along with a lipid sheath. Picodiscs employ the protein saposin A, which naturally functions to facilitate lipid degradation in the lysozome. Saposin A-amphiphile complexes therefore tend to be most stable at acidic pH, which is not optimal for most membrane protein applications. In search of new picodisc assemblies, we have explor","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-02T22:40:10.858Z","creation":"2025-04-06T01:53:58.385Z"},"accession":"S-EPMC8044043","cross_references":{"pubmed":["33755420"],"doi":["10.1021/acs.biochem.0c00924"]}}