Peptide and protein drug analysis
Book information
Description
Furthering efforts to simulate the potency and specificity exhibited by peptides and proteins in healthy cells, this remarkable reference supplies pharmaceutical scientists with a wealth of techniques for tapping the enormous therapeutic potential of these molecules-providing a solid basis of knowledge for new drug design. Provides a broad, comprehensive overview of peptides and proteins as mediators of cell movement, proliferation, differentiation, and communication. Written by more than 50 leading international authorities, Peptides and Protein Drug Analysis ·discusses strategies for dealing with the complexity of peptides and proteins in conformational flexibility and amino acid sequence variability ·analyzes drug formulations facilitated by solid-phase peptide synthesis and recombinant DNA technology ·examines chemical purity analysis by high-pressure chromatographic, capillary electrophoretic, gel electrophoretic, and isoelectric focusing methods ·highlights drug design elements derived from protein folding, bioinformatics, and computational chemistry ·demonstrates uses of unnatural mutagenesis and combinatorial chemistry ·explores mass spectrometry, protein sequence, and carbohydrate analysis ·illustrates bioassays and other new functional analysis methods ·surveys spectroscopic techniques such as ultraviolet, fluorescence, Fourier transform infrared, and nuclear magnetic resonance (NMR) ·addresses ways of distinguishing between levels of therapeutic and endogenous agents in cells ·reviews structural analysis tools such as ultracentrifugation and light, X-ray, and neutron scattering ·and more! Featuring over 3400 bibliographic citations and more than 500 tables, equations, and illustrations, Peptide and Protein Drug Analysis is a must-read resource for pharmacists; pharmacologists; analytical, organic, and pharmaceutical chemists; cell and molecular biologists; biochemists; and upper-level undergraduate and graduate students in these disciplines.
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