Peptide and Protein Design for Biopharmaceutical Applications


Book Description

Peptides serve as effective drugs in the clinic today. However the inherent drawbacks of peptide structures can limit their efficacy as drugs. To overcome this researchers are developing new methods to create ‘tailor-made’ peptides and proteins with improved pharmacological properties. Design of Peptides and Proteins provides an overview of the experimental and computational methods for peptide and protein design, with an emphasis on specific applications for therapeutics and biomedical research. Topics covered include: Computer modeling of peptides and proteins Peptidomimetics Design and synthesis of cyclic peptides Carbohydrates in peptide and protein design De novo design of peptides and proteins Medical development applications An extended case study – the design of insulin variants Design of Peptides and Proteins presents the state-of-the-art of this exciting approach for therapeutics, with contributions from international experts. It is an essential resource for academic and industrial scientists in the fields of peptide and protein drug design, biomedicine, biochemistry, biophysics, molecular modelling, synthetic organic chemistry and medicinal/pharmaceutical chemistry.




Biologically Active Peptides


Book Description

Investigation into basic and advanced peptide design, synthesis, evaluation and utilization. New therapeutic approaches from experimental systems.




Biophysical Characterization of Functional Peptides


Book Description

This protocol book presents reproducible and step-by-step procedures for the peptide synthesis, their characterization and applications. The volume includes an introductory section on in silico modelling of new peptide molecules, Molecular Dynamics Simulations, Docking, Electrostatic fingerprinting of peptides, and other modelling tools for peptide designing and optimization. Further, it covers protocols for the solid phase peptide synthesis, chromatographic and mass spectrometric characterization of peptides. Importantly, it covers methods for biophysical characterizations of peptides for their potential applications as drug delivery vehicles, peptide nano-assembly, bionanocatalysis, protein aggregation diseases, and peptide-based anti-bacterial. ​




Conformation in Biology and Drug Design


Book Description

The Peptides: Analysis, Synthesis, Biology, Volume 7: Conformation in Biology and Drug Design focuses on the analysis of peptides, emphasizing the use of physical methods in peptide conformational analysis and the relationship of conformational properties of peptides to biological properties. This book consists of nine chapters. Chapter 1 provides a brief overview of the perspective on the application of physical methods to peptide conformational analysis. The use of circular dichroism (CD) spectroscopy to examine the conformational properties of peptides in solution is elaborated in Chapter 2, while the use of fluorescence spectroscopy to examine the special relationships of aromatic side-chain groups to one another is discussed in Chapter 3. In Chapter 4, the use of various theoretical methods to calculate the conformations of peptides is described. The methods used to stimulate peptide conformations and dynamics are outlined in Chapter 5. The last four chapters examine various aspects of the use of nuclear magnetic resonance (NMR) in peptide conformational analysis. This volume is suitable for biologists, specialists, and researchers interested in peptides and proteins.







The Design, Synthesis, and Characterization of Novel Alanine-rich Polypeptides with Varied Functional Group Density


Book Description

These polypeptides were designed to be used in biological applications, and the aggregation behavior of the polypeptides was monitored via analytical ultracentrifugation and electrophoresis under physiologically relevant salt conditions (pH 2.3, 10 mM phosphate, 150 mM NaCl or pH 7.4 PBS). Because of the hydrophobic nature of the sequence, 65-H-2 displays high levels of association in pH 2.3, 10 mM phosphate, 150 mM NaCl buffer, and low levels of association are also seen in pH 7.4 PBS buffer. The less hydrophobic sequences, 17-H-3, 17-H-6, and 35-H-6, do not aggregate in pH 7.4 PBS. The ability to manipulate the conformational behavior and association of the polypeptides via changes in salt, polypeptide concentration, and temperature allows these polypeptides to be tailored for specific applications in materials science or biology.