University of California

Heather D Maynard

Natalie Boehnke

Rock J Mancini

Juneyoung Lee

Thi Nguyen

En-Wei Lin

Leonard H Rome

Tatiana Segura

Alexander M Spokoyny

Jonathan Lam

Gregory Grover

Alejandra Gonzalez

Samantha J Paluck

Debora Bontempo

Elaine A Qian

Marco S Messina

Alex Wixtrom

Daniel Buehler

Jonathan Axtell

Kent Kirlikovali

Trehalose-based nanogels for stabilizing and controlled releasing biomolecules such as glucagons are disclosed. Specifically, trehalose-based nanogels comprise (a) a copolymer comprising first methacrylate units and second methacrylate units, wherein (i) the first methacrylate units comprise trehalose side chains; and (ii) the second methacrylate units comprise disulfide side chains; (b) dithiol cross-linkers; wherein the dithiol cross-linkers cross link the copolymer through the disulfide side chains of the second methacrylate units.

Stabilization of glucagon by trehalose glycopolymer nanogels

An enzyme-responsive peptide and a method off using such enzyme-responsive peptide are disclosed. An enzyme-responsive peptide, the peptide comprising an amino acid having an α-amino group, an α-carboxylic acid group and a ε-amine group, wherein the ε-amine group is covalently bonded with a first group and the α-carboxylic acid is covalently bonded with a second group.

Dual-enzyme responsive peptides

Non-crushable pill formulations and methods of using the formulations are disclosed. A non-crushable pill formulation for preventing unintended use of a drug, comprising a polymer, the polymer forming a polymer backbone of the complex; cross-linkers, the cross-linkers connecting the polymer backbone through covalently bonding to form at least one inner cavity within the complex; and the drug, the drug being trapped either covalently or non-covalently in the at least one inner cavity within the complex, wherein the drug is protected from releasing outside of the complex.

Noncrushable pill formulations

Novel three-dimensional molecular clusters and methods of their synthesis are provided. The three-dimensional molecular clusters may be perfunctionalized polyhedral boranes and carboranes. The three-dimensional clusters may be configured to manipulate the photophysical properties of other materials, including, for example, for use as photooxidants or as components in organic light-emitting diode materials. Methods are also provided for synthesizing and perfunctionalizing such three-dimensional clusters. The three-dimensional clusters may also be configured for use as organomimetic materials.

Three-dimensional boron-rich clusters

Structures and methods of making biodegradable trehalose co-polymers are disclosed. Specifically, biodegradable trehalose co-polymers consist of the general structure R&#x2014;[RRC&#x2014;CRR]n-[DG]-R, wherein R-Rare independently selected from hydrogen or a side chain comprising at least one carbon atom, and wherein at least one of R-Ris a side chain comprising -L-trehalose, wherein L is a linker molecule that links trehalose to the monomer through at least one of the trehalose hydroxyl groups (&#x2014;OH), wherein DG is a biodegradable group, and wherein Rand Rare end groups.

Biodegradable trehalose glycopolymers

The invention relates to compositions of vault complexes for use as delivery agents for hydrophobic and/or aqueous insoluble therapeutic compounds. In one aspect, provided herein is a vault complex comprising a modified major vault protein (MVP), wherein the modified major vault protein comprises a fusion peptide, wherein said fusion peptide is fused to the N-terminus of the major vault protein, and wherein said peptide provides enhanced sequestering of a hydrophobic and/or aqueous insoluble therapeutic compound within the vault complex.

Vaults engineered for hydrophobic drug delivery

Trehalose-based hydrogels and methods of making such hydrogels are disclosed. Specifically, a method of creating a trehalose-based hydrogel, comprising the steps of: a) forming a trehalose homopolymer or co-polymer; b) preparing a cross-linker; and c) reacting the trehalose homopolymer or co-polymer with the cross-linker to form the trehalose-based hydrogel.

Trehalose hydrogels for stabilization and delivery of proteins

Compositions and methods for stabilizing biomolecules are disclosed. Specifically, the compositions include novel homopolymers or copolymers containing trehalose side chains conjugated to biomolecules. When such homopolymers or copolymers are placed in close proximity to biomolecules, such as proteins, the homopolymers or copolymers protect and/or stabilize the biomolecule. The compositions and methods may be suitable for use in various industries such as healthcare (pharmaceuticals), molecular biology, biofuels, paper, personal care, detergent, photographic, rubber, brewing, dairy and food processing industries.

Stabilization of biomolecules using sugar polymers

Structures and methods of making biodegradable trehalose co-polymers are disclosed. Specifically, biodegradable trehalose co-polymers consist of the general structure R&#x2014;[RRC&#x2014;CRR]-[DG]&#x2014;R, wherein R-Rare independently selected from hydrogen or a side chain comprising at least one carbon atom, and wherein at least one of R-Ris a side chain comprising -L-trehalose, wherein L is a linker molecule that links trehalose to the monomer through at least one of the trehalose hydroxyl groups (&#x2014;OH), wherein DG is a biodegradable group, and wherein Rand Rare end groups.

Substituted polyesters by thiol-ene modification: rapid diversification for therapeutic protein stabilization

A method of creating a hydrogel, comprising the step of condensing first and second functional groups, wherein the first group comprises a molecule or macromolecule of interest containing two or more hydroxylamine or aminooxy groups and the second group comprises a molecule or macromolecule of interest containing two or more aldehyde/ketone/other reactive oxo groups, under conditions such that a hydrogel forms.

Method of creating hydrogels through oxime bond formation

A heparin mimicking polymer, its conjugate with bFGF, and method of making and using the same are disclosed. In particular, described herein are conjugates of biologic agents (e.g., bFGF) and heparin mimicking polymers having superior stability while retaining full native activity after a variety of stressors.

bFGF-polymer conjugates, methods for making the same and applications thereof

Chemical polymerization procedures initiated by, and proceeding from, a biomolecule, particularly a protein, for the formation of biomolecule-polymer conjugates, particularly protein-polymer conjugates, which have therapeutic uses, are intermediates for forming other materials or are usable in diagnostic sensors are disclosed. Polymerization can be initiated by a protein in the absence of additional initiation agents to form the protein-polymer conjugate. Alternatively, polymerization is initiated in the presence of an additional initiation agent that does not interact with the protein. Amino acids existing in the protein can serve as the sites for initiation of the polymerization or the protein can be modified to contain site(s) for initiation or protein with active sites can be prepared by recombinant methods, chemical ligation, solid-phase synthesis, or other techniques to generate site(s) for initiation.

Growing community of inventors

Los Angeles, CA, United States of America

Heather D Maynard