C07K5/00

PROPYL CATIONIC PEPTIDE LIPIDS, SYNTHESIS METHOD THEREOF, AND APPLICATION THEREOF
20170355667 · 2017-12-14 ·

A class of propyl cationic peptide lipids is propyl cationic peptide lipid compounds having a general formula structure as follows. After the propyl cationic peptide lipids are dispersed in water, a cationic liposome with a particle size of approximately 100 nm is obtained. The cationic liposome can carry plasmid DNA (pDNA) or small interfering RNA (siRNA) into cells to realize the function of gene delivery, and is almost non-toxic to the cells.

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PROPYL CATIONIC PEPTIDE LIPIDS, SYNTHESIS METHOD THEREOF, AND APPLICATION THEREOF
20170355667 · 2017-12-14 ·

A class of propyl cationic peptide lipids is propyl cationic peptide lipid compounds having a general formula structure as follows. After the propyl cationic peptide lipids are dispersed in water, a cationic liposome with a particle size of approximately 100 nm is obtained. The cationic liposome can carry plasmid DNA (pDNA) or small interfering RNA (siRNA) into cells to realize the function of gene delivery, and is almost non-toxic to the cells.

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Somatostatin receptor agonist formulations
11672843 · 2023-06-13 · ·

The present invention relates to compositions forming a low viscosity mixture of: a) 20-50 wt. % of at least one diacyl glycerol; b) 20-54 wt. % of at least one phosphatidyl choline (PC); c) 5-15 wt. % of at least one biocompatible, organic mono-alcoholic solvent; d) 1 to 20 wt. % polar solvent e) 5 to 150 mg/ml of at least one peptide somatostatin receptor agonist comprising pasireotide; f) optionally at least one antioxidant; wherein the ratio of components a:b is in the range 40:60 to 54:46; wherein the pre-formulation forms, or is capable of forming, at least one liquid crystalline phase structure upon contact with excess aqueous fluid. The invention further relates to methods of treatment comprising administration of such compositions, and to pre-filled administration devices and kits containing the formulations.

Methods for treating heart disease in a subject with Friedreich's ataxia by an aromatic-cationic peptide
11672841 · 2023-06-13 · ·

The disclosure provides methods of preventing or treating Friedreich's ataxia in a mammalian subject, reducing risk factors, signs and/or symptoms associated with Friedreich's ataxia, and/or reducing the likelihood or severity of Friedreich's ataxia. The methods comprise administering to the subject an effective amount of an aromatic-cationic peptide to e.g., reduce oxidative stress, increase mitochondrial metabolism, or a combination thereof.

Compositions and method for optimized peptide vaccines using residue optimization

Described herein is an immunogenic composition comprising nucleic acid sequences encoding two or more amino acid sequences selected from the group consisting of SEQ ID NOs: 19 to 50. Also described herein is an immunogenic composition comprising nucleic acid sequences encoding two or more amino acid sequences selected from the group consisting of SEQ ID NOs: 141 to 272. Also described herein is an immunogenic composition comprising nucleic acid sequences encoding two or more amino acid sequences selected from the group consisting of SEQ ID NOs: 273 to 322. Also described herein is an immunogenic composition comprising nucleic acid sequences encoding two or more amino acid sequences selected from the group consisting of SEQ ID NOs: 354 to 458.

Hepcidin analogues and uses thereof

The present invention relates, inter alia, to certain hepcidin peptide analogs, including peptides and dimers thereof, and to the use of the peptides and peptide dimers in the treatment and/or prevention of a variety of diseases, conditions or disorders, including treatment and/or prevention of iron overload diseases, which include hereditary hemochromatosis and iron-loading anemias, and other conditions and disorders described herein.

Methods of making carfilzomib and intermediates thereof

Racemization-free methods are disclosed for the synthesis of carfilzomib. Novel intermediates and methods of making carfilzomib employing fragment condensation using the novel intermediates are disclosed. Amorphous carfilzomib and methods of making same are disclosed.

Crystalline bis- and tris-hydrochloride salt of elamipretide
11261213 · 2022-03-01 · ·

Disclosed are crystalline forms of the bis- and tris-(hydrochloride) salts of D-Arg-Tyr(2,6-DiMe)-Lys-Phe-NH.sub.2, which is also known as MTP-131.

Functional peptides for obesity disorders

The present invention concerns certain peptides obtainable by hydrolysis from soy glycinin by the action of supernatant cultures of strains belonging to the genera Lactobacillus or Streptococcus. These peptides, extracts containing them and food products containing them are useful for the treatment and/or prevention of obesity and oxidative stress.

SRM/MRM assay for the fatty acid synthase protein

Specific peptides, and derived ionization characteristics of the peptides, from the Fatty acid synthase (FASN) protein are provided that are particularly advantageous for quantifying the FASN protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the FASN protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an FASN peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.