Described herein is an operationally simple, one-pot solid-supported preparation of saturated stapled peptides. Following completion of ruthenium-catalysed metathesis, solid-phase transfer hydrogenation was achieved using triethylhydrosilane at elevated temperatures. The utility of the method has been demonstrated on 14- and 16-mer peptides to yield the corresponding cyclic a-helix stabilised stapled peptides.

The present invention relates to the formation of conjugates (e.g., protein-protein dimers) using a-halo-acetophenones, benzylic halides, quinones, and related compounds as a conjugating system. The invention also features compositions that include the conjugates described herein, as well as uses of these conjugates in methods of medical treatment.

A natural protein, specifically silk fibroin or sericin, is chemically modified such that it can be rendered photoactive, but which otherwise has similar structure and attributes as silk fibroin or sericin. This chemically modified silk conjugate can be patterned using radiant energy to produce patterned silk materials which may be used for a wide variety of applications such as making micro and nanoparticles of different shapes and functionalities for drug delivery, creating new forms of intricate 3D scaffolds for tissue engineering, and forming substrates for flexible bio-electronics.

A method for producing a ribosome display complex includes obtaining a ribosome complex including an unmodified polypeptide chain, an mRNA molecule and a ribosome by initiating translation of the mRNA molecule in a cell-free peptide synthesis system including the ribosome, and modifying the unmodified polypeptide chain by reacting a side chain reactive functional group in the unmodified polypeptide chain with a modifying reagent to produce a ribosome display complex including a modified polypeptide chain, the mRNA molecule and the ribosome. The unmodified polypeptide chain includes at least one reactive amino acid residue selected from the group consisting of a cysteine residue, a lysine residue, a histidine residue and a tryptophan residue. The at least one reactive amino acid residue includes the side chain reactive functional group, and the mRNA molecule includes a base sequence encoding an amino acid sequence of the polypeptide chain.

The present invention relates to cyclic amino acid molecules and methods of preparing the same, and in particular the macrocyclization of amino acids or linear peptides bound to a solid support.

The present invention relates to the field of medicinal synthesis, and discloses a method for synthesizing degarelix. The method of the present invention as a whole divides the synthesis of degarelix into two parts from amino acids at positions 5 and 6, employs proper protective groups in part of the protected amino acids therein, and finally uses in association with a specific acidolysis agent to complete the whole synthesis process. In the present invention, a proper synthesizing scheme is selected, and adaptive protective group and acidolysis agent are selected, so that the overall synthesis process is optimized, the purity of degarelix is significantly improved with a higer total yield, and the production of the toxic hydantoin degradation product is avoided.

Reactive nanocomposites comprising a metal nanoparticle functionalized with one or more layers of self-assembled protein cages and methods of making the same. The reactive nanocomposites according to the present invention demonstrate improved reaction kinetics and enhanced exothermic behavior.

The present disclosure provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a biological macromolecule comprising one or more thiol groups; and (b) a molecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure also provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a molecule comprising one or more thiol groups; and (b) biological macromolecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure further provides a covalently modified biological macromolecule prepared by any of disclosed methods. The covalently modified biological macromolecules may be further crosslinked to form a scaffold.

Methods for the preparation of sample polypeptide fractions are described. Sample polypeptides may be isolated from any of a variety of sources, including biological and non-biological systems. Sample polypeptides may be coupled or conjugated to other molecules to permit characterization of the sample polypeptide fractions. Sample polypeptide fractions may be prepared for analysis by a polypeptide assay.

The present invention relates to hydrogels prepared using silylated organic molecules (such as silylated biomolecules), a process for obtaining the same, and uses thereof.