Materials and methods for the design of hybrid materials comprising a conducting matrix, organic modifiers/linkers and modifying molecules.

The present invention provides methods of preparing a peptide having an N-terminal histidine, and compositions comprising a plurality of peptides prepared by the methods. The methods disclosed herein reduce racemization of the N-terminal histidine in the peptides during the synthesis process, thereby improving the yield and purity of the peptide compositions. Exemplary peptides that can be manufactured with the methods include Exenatide, Lixisenatide, and Liraglutide.

The present invention provides methods of preparing a peptide having an N-terminal histidine, and compositions comprising a plurality of peptides prepared by the methods. The methods disclosed herein reduce racemization of the N-terminal histidine in the peptides during the synthesis process, thereby improving the yield and purity of the peptide compositions. Exemplary peptides that can be manufactured with the methods include Exenatide, Lixisenatide, and Liraglutide.

The present invention is useful in screening for biomarkers associated with any other disease or condition. Such diseases and conditions range from the neurological diseases, autoimmune diseases and cancers identified above as well as any other disease or condition that has a biomarker such as an antibody or other characterizing protein or biomolecule associated with the disease or progression of the disease. The large ligand libraries of the invention can be used directly in biological fluid, under the appropriate experimental conditions and according to the processes recited herein, to screen for such markers and without the need to use fewer support members (e.g. about 100,000 or less) or without the need to transfer such peptoids or ligands to a microarray before screening the biological fluid. In addition, the ligand libraries may also be used to screen for cell based receptors that specifically relate to a particular cell surface marker.

A method for producing a polypeptide, includes at least one native ligation step using a peptide functionalized with a selenium group. The selenium peptides and compounds are also described.

Provided is an antimicrobial peptide Sparamosin from Scylla paramamosain. The Sparamosin mature peptide and its functional domain Sparamosin.sub.26-54 were synthesized by solid-phase synthesis with a purity of over 95%. Both Sparamosin and Sparamosin.sub.26-54 exhibit strong antimicrobial activity. More importantly, Sparamosin.sub.26-54 has strong antifungal activity and could inhibit the growth of a variety of yeasts and filamentous fungi. Based on the potent antimicrobial activities of Sparamosin and Sparamosin.sub.26-54, both peptides could be developed as alternatives for conventional antibiotics, antimicrobial agents, feed additives in aquaculture and livestock, preservatives, and mold inhibitors.

The present disclosure provides a method of solid-phase peptide synthesis from the N terminus to C terminus without detectable epimerization of the C-terminal amino acid. The method includes using derivatized amino acids comprising a diamino-aryl group.

Proteins containing a C-terminal thioester are important intermediates in semi-synthesis. Currently there is one main method for the synthesis of protein thioesters that relies upon the use of engineered inteins. The invention involves, in some aspects a method, utilizing Sortase A, for preparation of recombinant proteins containing a C-terminal .sup.αthioester. This new method for double ligatation is useful for synthesizing new or naturally occurring molecules such as a protein thioester.

A method for producing a purified peptide from a supported crude peptide having a support and a first peptide chain bonded to the support at the C-terminus. The method includes: introducing a linker and a hydrophilic unit to an amino group of the first peptide chain of the supported crude peptide; cleaving a bond between the first peptide chain and the support before or after at least one of the linker and the hydrophilic unit is introduced to the amino group of the first peptide chain such that a support-free hydrophilized peptide is obtained; treating the support-free hydrophilized peptide by liquid chromatography; and cleaving a bond between the linker and the first peptide chain in the support-free hydrophilized peptide by chemical treatment after the liquid chromatography treatment such that a peptide including the first peptide chain is obtained.

A method for producing a purified peptide from a supported crude peptide having a support and a first peptide chain bonded to the support at the C-terminus. The method includes: introducing a linker and a hydrophilic unit to an amino group of the first peptide chain of the supported crude peptide; cleaving a bond between the first peptide chain and the support before or after at least one of the linker and the hydrophilic unit is introduced to the amino group of the first peptide chain such that a support-free hydrophilized peptide is obtained; treating the support-free hydrophilized peptide by liquid chromatography; and cleaving a bond between the linker and the first peptide chain in the support-free hydrophilized peptide by chemical treatment after the liquid chromatography treatment such that a peptide including the first peptide chain is obtained.