neuropeptide-y and 1-(9-fluorenyl)methyl-chloroformate

neuropeptide-y has been researched along with 1-(9-fluorenyl)methyl-chloroformate* in 2 studies

Other Studies

2 other study(ies) available for neuropeptide-y and 1-(9-fluorenyl)methyl-chloroformate

Article	Year
Facile and selective nanoscale labeling of peptides in solution by using photolabile protecting groups. Journal of medicinal chemistry, 2003, Oct-09, Volume: 46, Issue:21 For the selective labeling of peptides, a novel strategy was developed that combines the advantages of solid-phase peptide synthesis with the flexibility of labeling reactions in solution. To direct a label at a distinct position within the peptide sequence, other reactive positions are blocked with photolabile protecting groups that could be easily removed after the labeling reaction. Therefore selective labeling may become feasible for the first time even in nanomol amounts. Topics: Animals; Calcitonin Gene-Related Peptide; Cells, Cultured; Chromatography, High Pressure Liquid; Cricetinae; Fluorenes; Humans; Indicators and Reagents; Nanotechnology; Neuropeptide Y; Peptides; Photochemistry; Receptors, Neuropeptide Y; Spectrophotometry, Ultraviolet; Ultraviolet Rays	2003
Investigation of crudes of synthesis of [Leu31, Pro34]-neuropeptide Y by capillary zone electrophoresis/mass spectrometry. Rapid communications in mass spectrometry : RCM, 1995, Volume: 9, Issue:14 [Leu31, Pro34]-Neuropeptide Y is a thirty-six amino-acid peptide which has a measured relative molecular mass of 4222. Solid-phase synthesis of this peptide resulted in complex crudes of synthesis which were examined by capillary zone electrophoresis (CZE)/electrospray ionization mass spectrometry (ES-MS). The separation efficiency of CZE combined with the mass specificity of mass spectrometry yielded rapid and reliable information on the target peptide and a number of associated side products, which were mainly acetylated peptide sequences having relative molecular masses in the range 2240-4101. Such incomplete or, as they are commonly called, difficult sequences are provoked by problems of swelling and aggregation of the growing peptide chains in the course of synthesis. The use of mass spectrometry is indispensable for obtaining reliable information on the inevitable side products. Initial tuning of the ion source and optimization of the coupling between the CZE system and the mass spectrometer were achieved by performing a number of measurements pertaining to artificially made mixtures of commercial neuropeptides. Topics: Amino Acid Sequence; Electrophoresis; Fluorenes; Indicators and Reagents; Mass Spectrometry; Molecular Sequence Data; Neuropeptide Y	1995

Article

Year

Facile and selective nanoscale labeling of peptides in solution by using photolabile protecting groups.

Journal of medicinal chemistry, 2003, Oct-09, Volume: 46, Issue:21

For the selective labeling of peptides, a novel strategy was developed that combines the advantages of solid-phase peptide synthesis with the flexibility of labeling reactions in solution. To direct a label at a distinct position within the peptide sequence, other reactive positions are blocked with photolabile protecting groups that could be easily removed after the labeling reaction. Therefore selective labeling may become feasible for the first time even in nanomol amounts.

Topics: Animals; Calcitonin Gene-Related Peptide; Cells, Cultured; Chromatography, High Pressure Liquid; Cricetinae; Fluorenes; Humans; Indicators and Reagents; Nanotechnology; Neuropeptide Y; Peptides; Photochemistry; Receptors, Neuropeptide Y; Spectrophotometry, Ultraviolet; Ultraviolet Rays

2003

Investigation of crudes of synthesis of [Leu31, Pro34]-neuropeptide Y by capillary zone electrophoresis/mass spectrometry.

Rapid communications in mass spectrometry : RCM, 1995, Volume: 9, Issue:14

[Leu31, Pro34]-Neuropeptide Y is a thirty-six amino-acid peptide which has a measured relative molecular mass of 4222. Solid-phase synthesis of this peptide resulted in complex crudes of synthesis which were examined by capillary zone electrophoresis (CZE)/electrospray ionization mass spectrometry (ES-MS). The separation efficiency of CZE combined with the mass specificity of mass spectrometry yielded rapid and reliable information on the target peptide and a number of associated side products, which were mainly acetylated peptide sequences having relative molecular masses in the range 2240-4101. Such incomplete or, as they are commonly called, difficult sequences are provoked by problems of swelling and aggregation of the growing peptide chains in the course of synthesis. The use of mass spectrometry is indispensable for obtaining reliable information on the inevitable side products. Initial tuning of the ion source and optimization of the coupling between the CZE system and the mass spectrometer were achieved by performing a number of measurements pertaining to artificially made mixtures of commercial neuropeptides.

Topics: Amino Acid Sequence; Electrophoresis; Fluorenes; Indicators and Reagents; Mass Spectrometry; Molecular Sequence Data; Neuropeptide Y

1995