Abstract: A method of producing an anhydrous antiperspirant composition comprising (a) providing a mixture of at least one antiperspirant active including a metal salt, and an anhydrous carrier for the at least one antiperspirant active in which the at least one antiperspirant active is dissolved, the carrier comprising a eutectic mixture of at least one basic compound selected from a basic amide and a basic amine and at least one member chosen from a cation and zwitterion; and (b) heating the mixture to form a stabilized eutectic system of the at least one antiperspirant active and the anhydrous carrier, and wherein the at least one antiperspirant active, the at least one basic compound and the at least one member chosen from a cation and zwitterion form a ternary eutectic system.

Abstract: A method of producing an anhydrous antiperspirant composition comprising (a) providing a mixture of at least one antiperspirant active including a metal salt, and an anhydrous carrier for the at least one antiperspirant active in which the at least one antiperspirant active is dissolved, the carrier comprising a eutectic mixture of at least one basic compound selected from a basic amide and a basic amine and at least one member chosen from a cation and zwitterion; and (b) heating the mixture to form a stabilized eutectic system of the at least one antiperspirant active and the anhydrous carrier, and wherein the at least one antiperspirant active, the at least one basic compound and the at least one member chosen from a cation and zwitterion form a ternary eutectic system.

Abstract: A method of producing an anhydrous antiperspirant composition comprising (a) providing a mixture of at least one antiperspirant active including a metal salt, and an anhydrous carrier for the at least one antiperspirant active in which the at least one antiperspirant active is dissolved, the carrier comprising a eutectic mixture of at least one basic compound selected from a basic amide and a basic amine and at least one member chosen from a cation and zwitterion; and (b) heating the mixture to form a stabilized eutectic system of the at least one antiperspirant active and the anhydrous carrier. Also, an anhydrous antiperspirant composition.

Abstract: An aqueous antiperspirant/deodorant composition comprising: (a) at least one active chosen from an antiperspirant active and a deodorant active, (b) a mixture comprising at least one basic compound chosen from a basic amide and a basic amine and a counterpart material for the basic amide and/or basic amine, and (c) at least 10 weight % water. Also, a method of manufacturing the composition.

Abstract: An aqueous antiperspirant/deodorant composition comprising: (a) at least one active chosen from an antiperspirant active and a deodorant active, (b) a mixture comprising at least one basic compound chosen from a basic amide and a basic amine and a counterpart material for the basic amide and/or basic amine, and (c) at least 10 weight % water. Also, a method of manufacturing the composition.

Abstract: A method of producing an anhydrous antiperspirant composition comprising (a) providing a mixture of at least one antiperspirant active including a metal salt, and an anhydrous carrier for the at least one antiperspirant active in which the at least one antiperspirant active is dissolved, the carrier comprising a eutectic mixture of at least one basic compound selected from a basic amide and a basic amine and at least one member chosen from a cation and zwitterion; and (b) heating the mixture to form a stabilized eutectic system of the at least one antiperspirant active and the anhydrous carrier. Also, an anhydrous antiperspirant composition.

Abstract: An anhydrous liquid antiperspirant/deodorant composition comprising a carrier comprising a cation and/or zwitterion and a hydrogen bond donor, wherein an amount of carrier is greater than an amount of any other material in the composition, and an antiperspirant active. This represents a new delivery form for antiperspirant actives and/or deodorant actives.

Abstract: In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed.

Abstract: In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed.

Abstract: In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed.

Abstract: In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed.

Abstract: The present invention relates generally to systems and methods for determining differential protein expression, and diagnostic discovery systems and methods that utilize the same. In particular, the present invention relates to a system and method of obtaining and analyzing protein profiles to determine protein patterns associated with clinical parameters and manifestations of disease and to discover specific biomarkers that are characteristic of diseases such as cancer. The present invention further relates to the identification of potential molecular targets for diagnostic applications and/or therapeutic intervention.

Abstract: A cell protein profiling and diagnostic system is provided that fractionates a protein content of a tissue sample into protein subgroups, independently performs mass spectroscopy on each protein subgroup, creates a cell expression protein profile from the mass spectra, and identifies protein patterns associated with subject characteristics, such as biological conditions and diseases, based on the cell expression protein profile. In one embodiment, the protein patterns are identified with an artificial neural network, or other data mining or pattern recognition techniques.

Abstract: A protein signature analysis is obtained using a peptide ladder library. The molecular signature of a protein is defined to be that subsequence of amino acid positions within the protein which are essential for the protein to bind to a target molecule. The molecular signature may be determined by screening a peptide ladder library which corresponds to the protein against the target molecule. The peptide ladder library is a library of m peptides wherein each peptide has an amino acid sequence of length m corresponding to an amino acid sequence of the protein, with one exception, viz. peptidem has a substitute amino acid at positionm and the substitute amino acid is attached by a labile bond to its neighboring amino acid. Screening the peptide ladder library against the target molecule results in a division of the original mixture into a positive (functional) pool and a negative (non-functional) pool. The pools are separated and subjected to cleavage to obtain cleavage products.