Peptide history

In this Appendix biographical sketches are compiled of many scientists who have made notable contributions to the development of peptide chemistry up to its present state. We have tried to consider names mainly connected with important events during the earlier periods of peptide history, but could not include all authors mentioned in the text of this book. This is particularly true for the more recent decades when the number of peptide chemists and biologists increased to such an extent that their enumeration would have gone beyond the scope of this Appendix. 

LSBC has a long history of process development, scale-up and manufacturing experience, since its foundation back in 1987. The company has developed proprietary, industrial-scale extraction processes for the purification of proteins, peptides, and other biochemicals from plant biomass. It has also developed commercial methods for the extraction and purification of secreted plant proteins. 

No tandem MS experiment can be successful if the precursor ions fail to fragment (at the right time and place). The ion activation step is crucial to the experiment and ultimately defines what types of products result. Hence, the ion activation method that is appropriate for a specific application depends on the MS instrument configuration as well as on the analyzed compounds and the structural information that is wanted. Various, more or less complementary, ion activation methods have been developed during the history of tandem MS. Below we give brief descriptions of several of these approaches. A more detailed description of peptide fragmentation mles and nomenclature is provided in Chapter 2. An excellent review of ion activation methods for tandem mass spectrometry is written by Sleno and Volmer, see Reference 12, and for a more detailed review on slow heating methods in tandem MS, see Reference 13. 

Wieland, T., and Bodanszky, M. (1991) The world of peptides a brief history of peptide chemistry. 298pp. Springer-Verlag. 

Potential therapeutic applications of host defense peptides also include the lantibiotic nisin. Indeed, nisin has had an impressive history as a food preservative with FDA approval in 1988 for use in pasteurized, processed cheese spreads. The attractiveness of nisin as a potential therapeutic is also enhanced due to its relative resistance to proteases and broad spectrum Gram-positive antimicrobial activity including multidrug-resistant strains. Biosynexus Inc. has licensed the use of nisin for human clinical applications and Immucell Corp. has licensed the use of Mast Out, an antimastitic nisin-containing product, to Pfizer Animal Health." Indeed, nisin formulations have been used as an active agent in the topical therapies Mast Out and Wipe-Out for bovine mastitis, an inflammatory disorder of the udder that is the most persistent disease in dairy cows." ... 

Brownstein MJ, A brief history of opiates, opioid peptides, opioid receptors, Proc... 

Arentz-Hansen et al. (2004) ( continuation of Lundin et al, 2003) 9 CD subjects who had history of oats exposure ( 5/9 from same study population) Derivation of polyclonal T cell lines In vitro duodenal mucosal cultures were challenged with either pepsin or Avenin-reactive T cell lines recognized avenin peptides in the context of HLA-DQ2 A substantial proportion of the avenin-reactive T cell appears to be specific to avenin Some CD patients have avenin-reactive mucosal T cells that can cause mucosal inflammation... 

For centuries opium was used for both medicinal and recreational purposes. Derived from the poppy Papaver somniferum, it contains numerous opiates, the primary one of which is morphine. The term opiate has largely been replaced by opioid, which represents all compounds with morphinelike activity and includes morphine, morphine derivatives, and peptides. Opiate is used to refer to morphinelike drugs derived from the plant and structurally similar analogues. These drugs are frequently referred to as narcotics, a Greek term for stupor, which is scientifically obsolete. Even in its early history, opium presented a problem when it was smoked or taken orally. The introduction of the hypodermic needle and syringe, however, drastically enhanced the euphoric properties of opioids and thereby altered their abuse liability. In addition, the synthesis of heroin resulted in an opioid that was more potent than morphine and ideally suited for intravenous administration. 

Brownstein, M.J. A brief history of opiates, opioid peptides, and opioid receptors, Proc. Natl. Acad. Sci. USA. 1993, 15, 5391-5393. 

The synthesis of peptidyl polymers has a long and elegant history, beginning with the construction of homopolypeptides and random copolypeptides. More recently, biomolecules that incorporate peptide entities into classic polymer structures have been created. Sequential peptide polymers have been constructed that model the three-dimensional structure of connective tissue proteins. This article describes methods for the assembly of a variety of peptidyl polymers. 

Enantiomerically pure amino adds owe their great importance among chiral compounds to the fact that not only are they among the most versatile building blocks with a rich and vast history of transformation to other products such as peptides, amino alcohols, amino aldehydes, and many others, but that most natural L-amino acids are important components of infusion solutions, health food, and animal feed preparations. For this reason, several processes exist on a large scale that are described in the following sections. 

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