Peptides are provided that are capable of inhibiting cell activation mediated by a Toll-like receptor (TLR) selected from TLR 1, 2, 4 or 6, said peptide comprising a sequence consisting of, or found within, the sequence of the transmembrane domain of a TLR selected from TLR 1, 2, 4 or 6 and optionally cytoplasmic and extracellular regions flanking the transmembrane domain. These peptides as well as pharmaceutical composition comprising them are useful for the treatment of TLR-mediated disease.

Novel analogues of the sea anemone Stichodactyla helianthus toxin ShK, and their use as, for example, therapeutic agents for treating autoimmune diseases are disclosed. The analogues comprise a ShK toxin polypeptide and an N-terminal extension comprising an amino acid sequence according to formula (I): wherein X.sup.−4 is D, E or other negatively-charged amino acid or derivative thereof, X.sup.−3 is E, I, L, S, V, W or a tryptophan derivative, X.sup.−2 is any amino acid, X.sup.−1 is any amino acid, a is absent or a first additional moiety, and b is absent or a second additional moiety.

a-X.sup.−4X.sup.−3X.sup.−2X.sup.−1-b (SEQ ID NO: 3)   (I)

Uranium-chelating polypeptides comprising at least one helix-loop-helix calcium-binding (EF-hand) motif which comprises a deletion of at least two amino acid in the 12-amino-acid calcium-binding loop sequence, and their use for uranium biodetection and biodecontamination.

The present disclosure provides a novel bridge peptide. The present disclosure provides a bridge peptide comprising a bridge moiety and a peptide moiety, wherein position β is tertiary or quaternary when the carbon at which the bridge moiety attaches to the peptide moiety is in position α. The present disclosure provides a novel bridge peptide, particularly a bridge peptide resulting from stably bridging a peptide that does not possess a hydrogen bond to induce or maintain a secondary structure, e.g., a peptide having a β-strand structure.

The present disclosure provides a novel bridge peptide. The present disclosure provides a bridge peptide comprising a bridge moiety and a peptide moiety, wherein position β is tertiary or quaternary when the carbon at which the bridge moiety attaches to the peptide moiety is in position α. The present disclosure provides a novel bridge peptide, particularly a bridge peptide resulting from stably bridging a peptide that does not possess a hydrogen bond to induce or maintain a secondary structure, e.g., a peptide having a β-strand structure.

Specific peptides, and derived ionization characteristics of the peptides, from the Fatty acid synthase (FASN) protein are provided that are particularly advantageous for quantifying the FASN protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the FASN protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an FASN peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.

Methods for concentrating biofuel precursors, including terpenes such as farnesyl and geranylgeranyl derivatives, are based on the prenylation of peptides in living organisms, such as plant or algae cells. Generally, an expression vector containing a gene encoding a small peptide with a preferred amino acid sequence is used to produce a transgenic organism. Expression of the gene in the cells produces a short peptide which is processed by the protein prenylation machinery of the cell. This results in a peptide-prenyl fusion in which a sesqui- or di-terpene molecule is attached to the peptide. Due to its small size and amphiphilic properties, this molecule forms micelles which allow the sesqui- or di-terpene to accumulate to high concentrations within the cell. The peptide-prenyl micelles are then extracted and purified for use preferably as a biofuel.

An isolated peptide is disclosed. The peptide comprises a titanium oxide binding amino acid sequence connected to a heterologous biologically active amino acid sequence via a beta sheet breaker linker, wherein: (i) the titanium oxide binding amino acid sequence is selected to bind coordinatively with titanium oxide; (ii) the titanium oxide binding amino acid sequence is selected to induce a beta sheet structure; and (ii) the titanium oxide binding amino acid sequence binds to titanium oxide with a higher affinity than said biologically active amino acid sequence binds to the titanium oxide under physiological conditions. Use of the peptides and titanium devices comprising same are also disclosed.

A conjugate consisting of an insulin-like growth factor-1 (IGF-I) variant and one or two poly(ethylene glycol) group(s), characterized in that said IGF-I variant has an amino acid alteration at up to three amino acid positions 27, 37, 65, 68 of the wild-type IGF-I amino acid sequence so that one or two of said amino acids is/are lysine and amino acid 27 is a polar amino acid but not lysine, is conjugated via the primary amino group(s) of said lysine(s) and said poly(ethylene glycol) group(s) have an overall molecular weight of from 20 to 100 kDa is disclosed. This conjugate is useful for the treatment of neurodegenerative disorders like Alzheimer's Disease.

A fusion protein including granzyme B, a cell penetrating peptide, a cleavage site, and a targeting moiety, a composition for cell membrane penetration comprising the fusion protein, and an anticancer composition comprising the fusion protein.