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assignee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_d07a4ddba85ae3e35ca0a6f85dad9f6d
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_45db32e0a5e03e531e38d3a66c46329d
classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K14-001
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-16
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classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-705
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-16
filingDate 2000-06-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_ab32efa5e24ac48d16e36736bc2a80e2
publicationDate 2001-01-11-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber WO-0102425-A2
titleOfInvention Peptide conjugates for the stabilization of membrane proteins and interactions with biological membranes
abstract The present invention provides a novel class of detergents referred to herein as lipopeptide detergents. Lipopeptide detergents comprise an amphipathic α-helical peptide having a hydrophobic or neutral face and a hydrophilic face. To each end of this peptide is covalently linked an aliphatic hydrocarbon tail, these aliphatic tails being linked thereto such that they associate with the hydrophobic or neutral face of the peptide. Lipopeptide detergents can advantageously be used to stabilize membrane proteins in the absence of a phospholipid bilayer in a manner that preserves the native conformation and permits the subsequent crystallization thereof.
isCitedBy http://rdf.ncbi.nlm.nih.gov/pubchem/patent/EP-1544209-A1
priorityDate 1999-06-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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