{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shandler SJ"],"funding":["NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["12378-81"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3155016"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["133(32)"],"pubmed_abstract":["The design of ?-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of ?-peptides was designed to stably insert in TM orientations in phospholipid bilayers. Their secondary structures and orientation in the phospholipid bilayer was characterized using biophysical methods. Computational methods were then devised to design a ?-peptide that targeted a TM helix of the integrin ?(IIb)?(3). The designed peptide (?-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro."],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Computational design of a ?-peptide that targets transmembrane helices."],"pmcid":["PMC3155016"],"funding_grant_id":["T32 GM008275","P01 HL040387","GM54616","R37 GM054616","HL40387","R37 GM054616-16","GM60610","R01 GM054616","P01 HL040387-16","R01 GM060610-06","R01 GM060610"],"pubmed_authors":["Gai F","Bennett JS","Shandler SJ","Smith-Dupont KB","Korendovych IV","DeGrado WF","Streu CN","Litvinov RI","Moore DT","Billings PC"],"additional_accession":[]},"is_claimable":false,"name":"Computational design of a ?-peptide that targets transmembrane helices.","description":"The design of ?-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of ?-peptides was designed to stably insert in TM orientations in phospholipid bilayers. Their secondary structures and orientation in the phospholipid bilayer was characterized using biophysical methods. Computational methods were then devised to design a ?-peptide that targeted a TM helix of the integrin ?(IIb)?(3). The designed peptide (?-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Aug","modification":"2020-10-29T12:07:02Z","creation":"2019-03-26T23:28:46Z"},"accession":"S-EPMC3155016","cross_references":{"pubmed":["21780757"],"doi":["10.1021/ja204215f"]}}