Abstract:
The present disclosure provides danoprevir/NS3a complex reader (DNCR) and grazoprevir/NS3a complex readers (GNCR) polypeptides, fusion proteins, and combinations and their use.
Abstract:
De novo designed multi-pass transmembrane polypeptides are described, that include 2 or more transmembrane domains that are each between 15 and 35 amino acids in length, include one or more polar residues, and include at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, or more hydrophobic amino acid residues.
Abstract:
The application discloses multimeric assemblies including multiple oligomeric substructures, where each oligomeric substructure includes multiple proteins that self-interact around at least one axis of rotational symmetry, where each protein includes one or more polypeptide-polypeptide interface (“O interface”); and one or more polypeptide domain that is capable of effecting membrane scission and release of an enveloped multimeric assembly from a cell by recruiting the ESCRT machinery to the site of budding by binding to one or more proteins in the eukaryotic ESCRT complex (“L domain”); and where the multimeric assembly includes one or more subunits comprising one or more polypeptide domain that is capable of interacting with a lipid bilayer (“M domain”), as well as membrane-enveloped versions of the multimeric assemblies.
Abstract:
Hyperstable constrained peptides and methods and apparatus for designing such peptides are provided. A computing device can determine a peptide backbone using a computing device. The computing device can place zero or more disulfide bonds in the peptide backbone. The computing device can design one or more peptide sequences based on the peptide backbone. The computing device can validate at least one validated peptide sequence of the one or more peptide sequences. An output can be generated based on the at least one validated peptide sequence.
Abstract:
The application discloses multimeric assemblies including multiple oligomeric substructures, where each oligomeric substructure includes multiple proteins that self-interact around at least one axis of rotational symmetry, where each protein includes one or more polypeptide-polypeptide interface (“O interface”); and one or more polypeptide domain that is capable of effecting membrane scission and release of an enveloped multimeric assembly from a cell by recruiting the ESCRT machinery to the site of budding by binding to one or more proteins in the eukaryotic ESCRT complex (“L domain”); and where the multimeric assembly includes one or more subunits comprising one or more polypeptide domain that is capable of interacting with a lipid bilayer (“M domain”), as well as membrane-enveloped versions of the multimeric assemblies.
Abstract:
Designed polypeptides having the amino acid sequence of SEQ ID NQ: 1 are described that bind with high affinity and selectivity to the influenza hemagglutinin protein, and which can be used for treating and/or limiting an influenza infection, as well as diagnosing an influenza infection and identifying candidate compounds for treating an influenza infection.
Abstract translation:描述了具有SEQ ID NO:1的氨基酸序列的设计的多肽,其以对流感血凝素蛋白的高亲和力和选择性结合,并且其可用于治疗和/或限制流感感染以及诊断流感感染 并鉴定用于治疗流感感染的候选化合物。
Abstract:
Disclosed herein are polypeptides that bind to the hemagglutinin protein of influenza virus, and which can be used for treating and diagnosing influenza infection.