Torrey Pines Institute for Molecular Studies

About: Torrey Pines Institute for Molecular Studies is a nonprofit organization based out in San Diego, California, United States. It is known for research contribution in the topics: Antigen & T cell. The organization has 2323 authors who have published 2217 publications receiving 112618 citations.

Equimolar multiple oligomer mixtures, especially oligopeptide mixtures

Abstract: A process for the synthesis of a complex mixture pool of solid support-coupled monomeric repeating unit compounds such as amino acid derivatives is disclosed in which the mixture pool contains an equimolar representation of reacted monomeric repeating unit compounds coupled. Also disclosed is a process for the stepwise synthesis of a complex mixture of coupled or free, unsupported oligomers such as oligopeptides. A set of self-solubilizing, unsupported mixed oligopeptides having one or more predetermined amino acid residues at one or more of the same, predetermined positions in the oligopeptide chain in which the set contains equimolar amounts of a plurality of different amino acid residues, preferably at least six different residues, at one or more of the same predetermined positions of the oligopeptide chain is also disclosed, as are methods of making and using the same.

New opioid peptides, peptidomimetics, and heterocyclic compounds from combinatorial libraries.

Abstract: Here we review the use of combinatorial libraries in opioid receptor assays. Following a brief description of the history of the combinatorial field, methods for the generation of synthetic libraries and the deconvolution of mixture-based libraries are presented. Case studies involving opioid assays used to demonstrate the viability of combinatorial libraries are described. The identification of new opioid peptides from combinatorial libraries is reviewed. The peptides found are composed of L-amino acids, D-amino acids, or L-, D-, and unnatural amino acids, and range from tetrapeptides to decapeptides. Likewise, new opioid compounds identified from peptidomimetic libraries, such as peptoids and alkylated dipeptides, and those identified from acyclic (e.g., polyamine, urea) and heterocyclic (e.g., bicyclic guanidine) libraries, are reviewed.

Neuropeptide-y ligands

Abstract: There are disclosed novel neuropeptide Y ligands having general formula (I) wherein the symbols W, A, D, R?1, R2, R3, R4? are further defined in the description. Compounds of formula (I) are agonists and antagonists of neuropeptide Y, and are therefore useful as regulators of neuropeptide Y activity and in treating disorders related thereto.

Administration of Recombinant Heat Shock Protein 70 Delays Peripheral Muscle Denervation in the SOD1(G93A) Mouse Model of Amyotrophic Lateral Sclerosis.

Abstract: A prominent clinical feature of ALS is muscle weakness due to dysfunction, denervation and degeneration of motoneurons (MNs). While MN degeneration is a late stage event in the ALS mouse model, muscle denervation occurs significantly earlier in the disease. Strategies to prevent this early denervation may improve quality of life by maintaining muscle control and slowing disease progression. The precise cause of MN dysfunction and denervation is not known, but several mechanisms have been proposed that involve potentially toxic intra- and extracellular changes. Many cells confront these changes by mounting a stress response that includes increased expression of heat shock protein 70 (Hsp70). MNs do not upregulate Hsp70, and this may result in a potentially increased vulnerability. We previously reported that recombinant human hsp70 (rhHsp70) injections delayed symptom onset and increased lifespan in SOD1G93A mice. The exogenous rhHsp70 was localized to the muscle and not to spinal cord or brain suggesting it modulates peripheral pathophysiology. In the current study, we focused on earlier administration of Hsp70 and its effect on initial muscle denervation. Injections of the protein appeared to arrest denervation with preserved large myelinated peripheral axons, and reduced glial activation.