Designing [alpha]/[beta]-peptide Foldamers to Target Diverse Protein Surfaces PDF Download
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![Designing [alpha]/[beta]-peptide Foldamers to Target Diverse Protein Surfaces PDF](https://books.google.com/books/content/images/frontcover/R3CFAQAACAAJ?fife=w150-h200)
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Languages : en
Pages : 1146
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![Designing [alpha]/[beta]-peptide Foldamers to Target Diverse Protein Surfaces PDF](https://books.google.com/books/content/images/frontcover/R3CFAQAACAAJ?fife=w80-h100)
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Languages : en
Pages : 1146
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![Development of [alpha]-helix-like [alpha]/[beta]/[upsilon] Foldamers PDF](https://books.google.com/books/content/images/frontcover/QP-VjwEACAAJ?fife=w80-h100)
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Languages : en
Pages : 588
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Helical peptidomimetics that contain non-natural amino acid residues, such as beta- and gamma-amino acid residues, are less prone to proteolytic degradation than are conventional peptides (composed exclusively of alpha-amino acid residues). However, the additional backbone atoms in beta- and gamma-residues relative to alpha-residues may increase backbone flexibility, and thereby increase the entropic penalty upon binding to a protein partner, resulting in decreased affinity for the targets. Ring-constrained beta- and gamma-amino acids have been developed to address this problem by pre-organizing the residues for helical conformations. This thesis details development of alpha-helix-like alpha/beta/gamma foldamers containing cyclic and/or acyclic beta- and gamma-amino acid residues. Chapters 2 and 3 discuss biophysical investigations of helical alpha/beta/gamma-peptides. Studies of the ring-constrained beta- and gamma-residues' effects on the helicity of alpha/beta/gamma-peptides suggest that beta(3)- and gamma(4)- amino acid residues differ in their intrinsic tendencies to adopt helical secondary structure, with gamma(4)-residues displaying a higher propensity than beta(3)- residues. Different acyclic gamma-residues, and different patterns of alpha, beta and gamma residues in the backbone have been explored. The results show that as long as cyclically constrained beta-amino acids are incorporated into alpha/beta/gamma-peptides, the alpha/beta/gamma-peptide helical propensity is not very sensitive to the nature of the acyclic gamma-amino acids used (although gamma(4)-amino acids are the best helix-adopting acyclic residues) or the pattern of residues within the backbone. Chapter 4 discusses efforts to establish an alpha + alpha/beta/gamma coiled-coil system for use in thermodynamic analysis of alpha + alpha/beta/gamma coiled-coil folding propensities. Chapter 5 discusses efforts toward developing functional alpha/beta/gamma-peptides to modulate apoptosis-regulating protein-protein interactions.
Author: George W. Gokel
Publisher: Elsevier
ISBN: 0128031999
Category : Science
Languages : en
Pages : 4627
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Book Description
Comprehensive Supramolecular Chemistry II, Second Edition, Nine Volume Set is a ‘one-stop shop’ that covers supramolecular chemistry, a field that originated from the work of researchers in organic, inorganic and physical chemistry, with some biological influence. The original edition was structured to reflect, in part, the origin of the field. However, in the past two decades, the field has changed a great deal as reflected in this new work that covers the general principles of supramolecular chemistry and molecular recognition, experimental and computational methods in supramolecular chemistry, supramolecular receptors, dynamic supramolecular chemistry, supramolecular engineering, crystallographic (engineered) assemblies, sensors, imaging agents, devices and the latest in nanotechnology. Each section begins with an introduction by an expert in the field, who offers an initial perspective on the development of the field. Each article begins with outlining basic concepts before moving on to more advanced material. Contains content that begins with the basics before moving on to more complex concepts, making it suitable for advanced undergraduates as well as academic researchers Focuses on application of the theory in practice, with particular focus on areas that have gained increasing importance in the 21st century, including nanomedicine, nanotechnology and medicinal chemistry Fully rewritten to make a completely up-to-date reference work that covers all the major advances that have taken place since the First Edition published in 1996
Author: Stefan Hecht
Publisher: John Wiley & Sons
ISBN: 3527611487
Category : Science
Languages : en
Pages : 456
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Book Description
This truly comprehensive treatise of foldamers, from synthesis to applications in bio-, material-, and nanoscience is at once an introduction to the topic, while providing in-depth accounts on various aspects clearly aimed at the specialist. The book is clearly structured, with the first part concentrating on structure and foldamer design concepts, while the second part covers functional aspects from properties to applications. The international team of expert authors provides overviews of synthetic approaches as well as analytical techniques.
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Languages : en
Pages : 0
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There are many strategies that target biomedically important protein-protein interactions, based on small molecules, antibodies, and peptides. Peptides have the advantages of selectively targeting the protein of interest through a broad distribution of multiple interactions, unlike small molecules, and being relatively small in size, unlike an antibody. However, peptides have the disadvantage of being rapidly degraded by proteases. The Gellman group has developed strategies to incorporate beta-amino acids into biomedically relevant peptides to create alpha/beta-peptides that have similar biological activity to the natural alpha-peptide but increased protease resistance. The first part of my thesis focuses on development of alpha/beta-peptides as inhibitors of HIV infection. The protein gp41 is a surface protein on the HIV virus that is responsible for fusion of the viral membrane to the host cell membrane. Helical alpha-peptides, based on the viral sequence, are potent infection inhibitors because they bind to gp41 and inhibit the fusion mechanism. I describe two design strategies, one involving cyclic beta-residue constraints and the other involving electrostatic side chain interactions of beta-residues, to preorganize a helical alpha/beta-peptide conformation. Both of these design strategies have proven effective in creating alpha/beta-peptides that are as active as a prototype alpha-peptide in cell-based HIV infectivity assays and more resistant to proteolysis in in vitro assays. The alpha/beta-peptides are also used as tools to probe the binding interface between inhibitory peptides and the target structure formed by gp41. The second part of my thesis focuses on development of alpha/beta-peptides as agonists of the GLP-1 receptor (GLP-1R). The natural agonist of GLP-1R, glucagon-like peptide-1 (GLP-1), has received attention as a therapeutic agent for type 2 diabetes. GLP-1 has a short half-life in the bloodstream (two minutes). My goal was to increase the biological stability of GLP-1 by incorporating unnatural beta-residues and alpha-residues into the sequence. I describe the design strategy for an effective GLP-1 analogue and the performance of this analogue in cell-based assays and animal studies.
Author: Ali Tavassoli
Publisher: Royal Society of Chemistry
ISBN: 178801569X
Category : Science
Languages : en
Pages : 357
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Book Description
Protein-protein interactions (PPI) are at the heart of the majority of cellular processes, and are frequently dysregulated or usurped in disease. Given this central role, the inhibition of PPIs has been of significant interest as a means of treating a wide variety of diseases. However, there are inherent challenges in developing molecules capable of disrupting the relatively featureless and large interfacial areas involved. Despite this, there have been a number of successes in this field in recent years using both traditional drug discovery approaches and innovative, interdisciplinary strategies using novel chemical scaffolds. This book comprehensively covers the various aspects of PPI inhibition, encompassing small molecules, peptidomimetics, cyclic peptides, stapled peptides and macrocycles. Illustrated throughout with successful case studies, this book provides a holistic, cutting-edge view of the subject area and is ideal for chemical biologists and medicinal chemists interested in developing PPI inhibitors.
Author: Melissa D. Boersma
Publisher:
ISBN:
Category :
Languages : en
Pages : 310
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Author: Michael D. Wendt
Publisher: Springer Science & Business Media
ISBN: 3642289657
Category : Science
Languages : en
Pages : 276
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Book Description
Michael D. Wendt Protein-Protein Interactions as Drug Targets Shaomeng Wang , Yujun Zhao , Denzil Bernard , Angelo Aguilar , Sanjeev Kumar Targeting the MDM2-p53 Protein-Protein Interaction for New Cancer Therapeutics Kurt Deshayes , Jeremy Murray , Domagoj Vucic The Development of Small-Molecule IAP Antagonists for the Treatment of Cancer John F. Kadow , David R. Langley , Nicholas A. Meanwell , Michael A. Walker , Kap-Sun Yeung , Richard Pracitto Protein-Protein Interaction Targets to Inhibit HIV-1 Infection Nicholas A. Meanwell , David R. Langley Inhibitors of Protein-Protein Interactions in Paramyxovirus Fusion – a Focus on Respiratory Syncytial Virus Andrew B. Mahon , Stephen E. Miller , Stephen T. Joy , Paramjit S. Arora Rational Design Strategies for Developing Synthetic Inhibitors of Helical Protein Interfaces Michael D. Wendt The Discovery of Navitoclax, a Bcl-2 Family Inhibitor
Author: Harald Tschesche
Publisher: Walter de Gruyter
ISBN: 3110252368
Category : Science
Languages : en
Pages : 379
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Book Description
This book presents a survey of recent developments in protein biochemistry. Top researchers in the field of protein biochemistry describe modern methods to address the challenges of protein purification by three-phase partitioning, and their folding and degradation by the functions of chaperones. The significance of peptide purity for fibril formation is addressed as well as the use of target oriented peptide arrays in palliative approaches in mucoviszidose. The design and application of protein epitope mimetics just as the structural resolving of the misfolding of various mutant proteins in serpinopathies enlarge our tools in resolving pathophysiological imbalances.
Author: William P. Jencks
Publisher: Courier Corporation
ISBN: 9780486654607
Category : Science
Languages : en
Pages : 866
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Book Description
Exceptionally clear coverage of mechanisms for catalysis, forces in aqueous solution, carbonyl- and acyl-group reactions, practical kinetics, more.
