Abstract: Provided herein are compounds, derivatives thereof, composition comprising one or more of said compounds and derivatives, and methods for prevention and/or treatment of microbial infections and/or related diseases or conditions. The present compounds and/or derivatives thereof can be represented by Formula (I): The present methods include administering to a subject an effective amount of one or more compounds of Formula (I). In one embodiment, said microbial infections are bacterial infections. More specifically, said bacterial infections are staphylococcal infections.

Abstract: Provided herein are compounds, derivatives thereof, composition comprising one or more of said compounds and derivatives, and methods for prevention and/or treatment of microbial infections and/or related diseases or conditions. The present compounds and/or derivatives thereof can be represented by Formula (II): The present methods include administering to a subject an effective amount of one or more compounds of Formula (II). In one embodiment, said microbial infections are bacterial infections. More specifically, said bacterial infections are staphylococcal infections.

Abstract: The present disclosure relates to the design and generation of stapled helical peptides that perturb protein-protein interactions (PPIs). The methods disclosed herein for preparing stapled peptides involve providing a peptide having a first amino acid that is functionalized with a salicylaldehyde ester side group and a second amino acid functionalized with a 1,2-hydroxyl amine side group; reacting the first and second amino acids to generate an N,O-benzylidene acetal moiety; and performing acidolysis of the resultant N,O-benzylidene acetal moiety to generate the stapled peptide. In many forms, the stapled helical peptides described herein are not hydrophobic.

Abstract: Described are design and generation of a set of novel cyclic lipopeptides as potential antibacterial agents. New daptomycin analogues are generated by chemical synthesis, which makes introduction of an unnatural amino acid and any modification into daptomycin possible.

Abstract: Compounds, compositions and methods for the preparation of peptide/protein conjugates, said method comprising a step of reacting a compound (2) represented by the formula (2) with a compound (3) represented by the formula (3) to obtain compound (1) represented by the formula (1), wherein R? represents substituent, and R represents H or at least one substituents. Also disclosed is a kit comprising the compound.

Abstract: The present disclosure relates to the design and generation of stapled helical peptides that perturb protein-protein interactions (PPIs). The methods disclosed herein for preparing stapled peptides involve providing a peptide having a first amino acid that is functionalized with a salicylaldehyde ester side group and a second amino acid functionalized with a 1,2-hydroxyl amine side group; reacting the first and second amino acids to generate an N,O-benzylidene acetal moiety; and performing acidolysis of the resultant N,O-benzylidene acetal moiety to generate the stapled peptide. In many forms, the stapled helical peptides described herein are not hydrophobic.

Abstract: Compounds, compositions and methods for the preparation of peptide/protein conjugates, said method comprising a step of reacting a compound (2) represented by the formula (2) with a compound (3) represented by the formula (3) to obtain compound (1) represented by the formula (1), wherein R? represents substituent, and R represents H or at least one substituents. Also disclosed is a kit comprising the compound.

Abstract: A method for the synthesis of daptomycin or a daptomycin analogue is carried out on a resin to form a linear precursor followed by a serine ligation macrocyclization in solution. Daptomycin analogues can differ from daptomycin by substitution of amino acids residues and/or deletion or addition of amino acid residues. Daptomycin analogues can include a different fatty acid in the side arm of the daptomycin analogue.

Abstract: A chemoselective chemical ligation method is disclosed. The method joins two peptide segments efficiently to produce a larger peptide or protein, by generating a natural peptide bond (Xaa-Ser and Xaa-Thr) at the ligation site (Xaa represents any 5 amino acid). The method requires two steps (FIG. 1 (a)): a) reacting the starting peptide(s) to form an acetal intermediate with an acetal group at the ligation site; b) converting said acetal intermediate to a desired peptide or protein with said natural peptide bond.

Abstract: A chemoselective chemical ligation method is disclosed. The method joins two peptide segments efficiently to produce a larger peptide or protein, by generating a natural peptide bond (Xaa-Ser and Xaa-Thr) at the ligation site (Xaa represents any 5 amino acid). The method requires two steps (FIG. 1 (a)): a) reacting the starting peptide(s) to form an acetal intermediate with an acetal group at the ligation site; b) converting said acetal intermediate to a desired peptide or protein with said natural peptide bond.