9-Fluorenylmethoxycarbonyl (Fmoc) amino acids were first used for solid phase peptide synthesis a little more than a decade ago. Since that time, Fmoc solid phase peptide synthesis methodology has been greatly enhanced by the introduction of a variety of solid supports, linkages, and side chain protecting groups, as well as by increased understanding of solvation conditions. These advances have led to many impressive syntheses, such as those of biologically active and isotopically labeled peptides and small proteins. The great variety of conditions under which Fmoc solid phase peptide synthesis may be carried out represents a truly "orthogonal" scheme, and thus offers many unique opportunities for bioorganic chemistry.

Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids

Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate.

3-(Acylamino)-5-phenyl-2H-1,4-benzodiazepines, antagonists of the peptide hormone cholecystokinin (CCK), are described. Developed by reasoned modification of the known anxiolytic benzodiazepines, these compounds provide highly potent, orally effective ligands selective for peripheral (CCK-A) receptors, with binding affinities approaching or equaling that of the natural ligand CCK-8. The distinction between CCK-A receptors on the one hand and CNS (CCK-B), gastrin, and central benzodiazepine receptors on the other is demonstrated by using the structure-activity profiles of the new compounds. Details of the binding of these agents to CCK-A receptors are examined, and the method of development of these compounds is discussed in terms of its relevance to the general problem of drug discovery.

Methods for drug discovery: development of potent, selective, orally effective cholecystokinin antagonists

A protein map of the smallest known self-replicating organism, Mycoplasma genitalium (Class: Mollicutes), revealed a high proportion of acidic proteins. Amino acid composition was used to putatively identify, or provide unique parameters, for 50 gene products separated by two-dimensional gel electrophoresis. A further 19 proteins were subjected to peptide-mass fingerprinting using matrix-assisted laser desorption ionisation-time of flight (MALDI-TOF) mass spectrometry and 4 were subjected to N-terminal Edman degradation. The majority of M. genitalium proteins remain uncharacterised. However, the combined approach of amino acid analysis and peptide-mass fingerprinting allowed gene products to be linked to homologous genes in a variety of organisms. This has allowed proteins to be identified prior to detection of their respective genes via the M. genitalium sequencing initiative. The principle of ‘hierarchical’ analysis for the mass screening of proteins and the analysis of microbial genomes via their protein complement or ‘proteome’ is detailed. Here, characterisation of gene products depends upon the quickest and most economical technologies being employed initially, so as to determine if a large number of proteins are already present in both homologous and heterologous species databases. Initial screening, which lends itself to automation and robotics, can then be followed by more time and cost intensive procedures, when necessary.

Progress with gene‐product mapping of the Mollicutes: Mycoplasma genitalium

Enzymatic synthesis of deoxyribonucleotides. iv. isolation and characterization of thioredoxin, the hydrogen donor from escherichia coli b.

/pdf/method-for-determination-of-the-amino-acid-sequence-in-3k7fduqsf7.pdf

Method for Determination of the Amino Acid Sequence in Peptides.

/pdf/preparation-of-phenyl-thiohydantoins-from-some-natural-amino-3fqahmiqms.pdf

Preparation of Phenyl Thiohydantoins from Some Natural Amino Acids.

/pdf/note-on-the-stepwise-degradation-of-peptides-via-phenyl-43ld0q8ixk.pdf

Note on the Stepwise Degradation of Peptides via Phenyl Thiohydantoins.

/pdf/technique-for-partition-chromatography-on-starch-4qw3s4zrq9.pdf

Technique for Partition Chromatography on Starch.

/pdf/the-splitting-of-the-porphyrin-protein-bonds-in-cytochrome-c-1njzs8i4xz.pdf

Pehr Edman

Papers

Method for Determination of the Amino Acid Sequence in Peptides.

Preparation of Phenyl Thiohydantoins from Some Natural Amino Acids.

Note on the Stepwise Degradation of Peptides via Phenyl Thiohydantoins.

Technique for Partition Chromatography on Starch.

The Splitting of the Porphyrin-protein Bonds in Cytochrome c.