The present invention relates to a stapled peptide, a preparation method thereof and the use thereof, and more specifically to an amphipathic alpha-helical stapled peptide comprising hydrophobic amino acids and hydrophilic amino acids, a preparation method thereof, and the use thereof for intracellular delivery of an active substance.

The present invention relates to the diagnosis and treatment of diseases expressing Fibronectin Extra Domain B (EDB) such as diseases characterized by tissue remodeling and/or angiogenesis, in particular cancerous diseases, such as head and neck, brain, colorectal, lung, prostate and breast cancer. More particularly, the invention concerns peptides targeting Fibronectin Extra Domain B.

The present disclosure relates to the field of molecular biology and more specifically to methods for detecting anti-carbamylated protein (anti-CarP) antibodies in the serum of rheumatoid arthritis (RA) patients.

The present invention provides means and methods for equipping a polypeptide of interest at its C-terminus with a versatile adaptor amino acid that allows the functionalization of the polypeptide of interest.

According to one aspect, the present disclosure provides a method of identifying a substrate of a transglutaminase using a peptide array comprising a plurality of peptides. The method includes the steps of contacting the peptides in the peptide array with the transglutaminase, allowing the transglutaminase to bind to the peptides, and identifying the substrate of the transglutaminase.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

The present invention relates to a compound for stabilizing enzymes, the use of said compound for stabilizing an enzyme, a composition comprising said compound, a method of preparing the composition comprising said compound, a detergent composition comprising said compound and a method of preparing said compound.

A method of providing a high concentration disulfide-linked caspase inhibitor-cell penetrating peptide conjugate is described. The method includes incubating a caspase inhibitor having one or more thiol groups with a reducing agent selected from dithiothreitol (DTT), 2-mercaptoethanol (2-ME) and tris(2-carboxyethyl)phosphine (TCEP) to provide a reduced caspase inhibitor, removing the reducing agent from the reduced caspase inhibitor, and conjugating the reduced caspase inhibitor with a cell-penetrating peptide by a disulfide linkage.

Provided are a method for the modification of a polypeptide and uses. The method comprises the following steps: (1) introducing an X into the N-terminus of a polypeptide, thereby obtaining X-polypeptide; (2) oxidizing the X into an aldehyde group; (3) adding a reducing agent, and covalently coupling the oxidation product obtained in step (2) with PEG, thereby obtaining a PEG-modified polypeptide, wherein X is threonine or serine. In the present application, a single component of PEG-modified polypeptide is obtained by introducing a threonine or serine into the N-terminus of the polypeptide, and deriving the amino alcohol structure at the ortho-position of the N-terminus of the polypeptide as an aldehyde group by using a high-specificity oxidation method and covalently coupling the aldehyde group with PEG. The method has a strong universality and a wide range of application, and the method for separating the modified polypeptide is simple and convenient, thereby improving the stability and the circulating half-life of the polypeptide.

The present invention relates to a cyclic peptide from a novel bone morphogenetic protein 2 (BMP2), a preparation method therefor and an application thereof. The cyclic peptide from the novel BMP2 is selected from one of the following cyclized polypeptides: 1. a cyclized polypeptide having the sequence of CKIPKASSVPTELSAISMLYLGPGGDWIVAC; and 2. a cyclized polypeptide of which the sequence has an 80% homology with the sequence defined in item 1. The present invention also relates to a preparation method for the cyclic peptide from the novel BMP2, and an application thereof in the preparation of the composite material for promoting the repair of large-sized bone defects.