The invention provides monomeric and oligomeric amyloid beta peptide isomers that are resistant towards fibrillogenesis and their use as screening reagents or antigens in methods and pharmaceutical preparations for the treatment of Alzheimer's disease and other conditions related to protein misfolding. The alanines at positions 21 and 30, in wild type amyloid beta peptide amino acid sequence, are according to the invention replaced by cysteins, which results in an intra molecular disulphide bond. The invention further provides transgenic animals expressing modified amyloid precursor proteins or amyloid beta peptides.

The invention provides reagents, methods, and compositions for studying protein-protein interactions. The inventive system and methods allow the analysis of protein-protein interactions in vivo and in vitro. Advantages offered by various embodiments of the inventive system and methods compared to existing photocrosslinking approaches include, for example, (i) novel reversible crosslinking reagents that allow easy isolation, purification, and enrichment of the crosslinked products; (ii) trifiuoromethyl phenyldiazirine- or perfluorinaled phenylazide-based photocrosslinking reagents that provide high specific labeling, no side product, and higher photocrosslinking efficiency; (iii) versatile spacer groups that allow systematic contact site mapping; (iv) novel methods for isolating, purifying, and detecting crosslinked products based on the reversible-link chemistry; and (v) the ability to study the interaction sites in vitro, in situ, or in vivo.

The invention provides reagents, methods, and compositions for studying protein-protein interactions. The inventive system and methods allow the analysis of protein-protein interactions in vivo and in vitro. Advantages offered by various embodiments of the inventive system and methods compared to existing photocrosslinking approaches include, for example, (i) novel reversible crosslinking reagents that allow easy isolation, purification, and enrichment of the crosslinked products; (ii) trifiuoromethyl phenyldiazirine- or perfluorinaled phenylazide-based photocrosslinking reagents that provide high specific labeling, no side product, and higher photocrosslinking efficiency; (iii) versatile spacer groups that allow systematic contact site mapping; (iv) novel methods for isolating, purifying, and detecting crosslinked products based on the reversible-link chemistry; and (v) the ability to study the interaction sites in vitro, in situ, or in vivo.

The present disclosure generally relates to genetic engineering of bacteria. More particularly, the present disclosure describes genetic engineering of E. coli to create mutant O-antigen ligase, as well as novel lipopolysaccharide molecules resulting from that genetic engineering. Methods for using those novel molecules are also described.

The present disclosure generally relates to genetic engineering of bacteria. More particularly, the present disclosure describes genetic engineering of E. coli to create mutant O-antigen ligase, as well as novel lipopolysaccharide molecules resulting from that genetic engineering. Methods for using those novel molecules are also described.

The present invention is aimed for providing a novel peptide with a high drug efficacy and strong effect, a medicament or external preparation comprising it, specifically a prophylactic or therapeutic for dermatitis, rhinitis or alopecia, or a hair growth stimulant, a hair growing agent, an antipruritic or a skin-care product. The present invention achieved said aim by providing a cyclic peptide having an amino acid sequence expressed by the Formula I or a derivative thereof or a pharmaceutically acceptable salt thereof, wherein the amino acid sequence does not have a peptide bond that is not between the amino acids constituting the amino acid sequence.

Peptide and peptides that may be covalently linked to a lipid and methods of using such peptides and lipopeptides to prevent or treat disease are disclosed herein.

Described is a dipeptide comprising a non-proteogenic amino acid, methods of making such and methods of using said dipeptide in a process of making a polypeptide or protein comprising one or more non-proteogenic amino acids.

Disclosed herein are methods for large-scale, high-throughput identification of protein-protein interactions and the topologies thereof under physiologically relevant conditions. In one aspect, the disclosure provides methods for identifying one or a plurality of interacting peptides within a biological system comprising obtaining a population of proteins cross-linked with a cleavable protein interaction reporter (PIR) cross-linker, cleaving the PIR crosslinker to produce released peptides and cleaved reporter ions, and analyzing the population of released peptides to identify interacting peptides. Also disclosed are methods for identifying candidate drug compounds, as well as methods of data processing and visualization of protein-protein interactions.

A formulation of a diluted amino acid segment is prepared by mixing an amino acid segment and a diluting agent to form a mixture. The mixture is serially diluted to produce a diluted formulation. The amino acid segment includes a peptide sequence that is the same as a portion of a longer peptide sequence found in a naturally occurring material. A homeopathic remedy can be prepared using the formulation.