A process for the linear synthesis of a gram-positive class II bacteriocin or a variant thereof is disclosed herein. The process comprises the stepwise addition of selected amino acids to a solid support; pseudoproline positioning and reopening; and cleavage of the gram-positive class II bacteriocin or the variant thereof from the solid support to provide a linear gram-positive class II bacteriocin or variant thereof; and in situ disulfide bond formation. Various applications and uses of the synthetic bacteriocins are also disclosed. The synthetic process can also be used to synthesize variants of bacteriocins by the selective substitution of one or more amino acids and/or additions and/or deletions of selected amino acids.

A process for the linear synthesis of a gram-positive class II bacteriocin or a variant thereof is disclosed herein. The process comprises the stepwise addition of selected amino acids to a solid support; pseudoproline positioning and reopening; and cleavage of the gram-positive class II bacteriocin or the variant thereof from the solid support to provide a linear gram-positive class II bacteriocin or variant thereof; and in situ disulfide bond formation. Various applications and uses of the synthetic bacteriocins are also disclosed. The synthetic process can also be used to synthesize variants of bacteriocins by the selective substitution of one or more amino acids and/or additions and/or deletions of selected amino acids.

A peptide synthesis instrument can be used for small scale peptide synthesis. The instrument can include several unique features, including a compression style reaction vessel permitting quick setup of the reaction vessel, a double reaction vessel system permitting efficient mixing without loss of solvent or solvent-to-resin contact, gravity-fed heated reservoirs establishing a fixed volume for delivery to the reaction vessel, fume-free solvent addition permitting solvent addition to fixed bottles, and an improved amino acid manifold assembly which reduces the number of components and increases the ease of use of the instrument. Each of these features improve upon the current state of the art in solid phase automated peptide synthesizers.

A method for preparing, in the internal volume of at least one channel, a monolithic support on which uranyl cations are immobilised. The method comprises: (a) activating the inner surface of the channel(s); (b) introducing, into the internal volume of the channel(s), a polymerisation solution comprising: a monomer comprising a phosphate group, at least one crosslinking agent, several solvents, and a radical polymerisation initiator; (c) polymerising the polymerisation solution; (d) rinsing the monolithic support obtained in step (c); and (e) contacting the monolithic support previously rinsed, with a solution comprising uranyl cations. A method for capturing proteins that selectively bind uranium by means of a monolithic support prepared by the above-mentioned method, as well as to a method for recovering proteins that selectively bind uranium with the capture method.

Various embodiments generally relate to intelligently designing aptameric peptides for binding with a specific receptor and forming aptameric peptide libraries with the designed peptides. The aptameric peptides libraries can be tissue-specific and be used in drug delivery and therapeutic applications, in which designed peptides can be implanted on exosome surfaces for exosomal cargo delivery to a specific tissue. Various embodiments of the present disclosure involve the use of a generative adversarial network (GAN) machine learning model configured (e.g., trained) and used to output designed peptides that are similar to pre-existing peptides of a peptide dataset but that specifically bind to a selected receptor and have various selected physiochemical properties. In various embodiments, GAN machine learning models may receive representations of the pre-existing peptides and may output representations of designed peptides according to peptide vectorization and encoding schemas based at least in part on the amino acids within a peptide.

The disclosure is directed to compounds and methods for preparing purified macrocyclic peptide using “catch-release” methods. These methods comprise reacting a free amino group of a resin-bound linear peptide with an azide- or alkyne-functionalized cap to form a resin-bound capped linear peptide having an azide- or alkyne-functionalized cap; cleaving the capped linear peptide from the resin to form a free capped linear peptide having an azide- or alkyne-functionalized cap; reacting the free capped linear peptide having an azide-functionalized cap with an alkyne-functionalized catch resin, or reacting the free capped linear peptide having an akynyl-functionalized cap with an azide functionalized catch resin, to form a catch-resin bound capped linear peptide; reacting the catch-resin bound capped linear peptide under conditions sufficient to effect macrocyclization of the linear peptide and release of the macrocyclic peptide from the catch resin.

The methods described herein provide a means of producing an array of spatially separated proteins. The method relies on covalently attaching each protein of the plurality of proteins to a structured nucleic acid particle (SNAP), and attaching the SNAPs to a solid support.

A peptide synthesis instrument can be used for small scale peptide synthesis. The instrument can include several unique features, including a compression style reaction vessel permitting quick setup of the reaction vessel, a double reaction vessel system permitting efficient mixing without loss of solvent or solvent-to-resin contact, gravity-fed heated reservoirs establishing a fixed volume for delivery to the reaction vessel, fume-free solvent addition permitting solvent addition to fixed bottles, and an improved amino acid manifold assembly which reduces the number of components and increases the ease of use of the instrument. Each of these features improve upon the current state of the art in solid phase automated peptide synthesizers.

The present invention relates to peptide modifier compounds of Formula (1), or a salt thereof, wherein: a is an integer from 1 to 10, more preferably from 1 to 3; b is an integer from 0 to 7; Z is a terminal group and Y is a bivalent group. Further aspects of the invention relate to intermediates in the preparation of compounds of Formula (1), and the use of compounds of Formula 1 in the synthesis of peptide derivatives. ##STR00001##

The present invention relates to peptide modifier compounds of Formula (1), or a salt thereof, wherein: a is an integer from 1 to 10, more preferably from 1 to 3; b is an integer from 0 to 7; Z is a terminal group and Y is a bivalent group. Further aspects of the invention relate to intermediates in the preparation of compounds of Formula (1), and the use of compounds of Formula 1 in the synthesis of peptide derivatives. ##STR00001##