Study of the peptide-peptide and peptide-protein interactions and their applications in cell imaging and nanoparticle surface modification. (2016)

• Record Type: Book
• Further Information: Note: Jianpeng Wang.
• Authors: Wang, Jianpeng
• Contents: Supervisor's Foreword; Parts of this thesis have been published in the following journal articles:; Acknowledgements; Contents; 1 Introduction; 1.1 Introduction to Chemical Biology; 1.2 Antimicrobial Peptides; 1.3 Quantum Dots; 1.4 Introduction to Chemical Tag and Probe System; 1.4.1 Classification of Covalent Chemical Tag and Probe System; 1.4.1.1 Labeling Methodologies Based on Single Amino Acid; 1.4.1.2 Labeling Strategies Based on Short Peptide Tag Sequence; 1.4.1.3 Labeling Methodologies Based on Fusion Proteins (Enzymes); 1.4.2 Noncovalent Tag and Probe System; References. 2 Biological Active Antifungal Peptides2.1 Introduction; 2.2 Experimental Section; 2.2.1 Peptide Synthesis and Purification; 2.2.2 Intermolecular Disulfide Bond Formation; 2.2.3 Intramolecular Disulfide Bond Formation; 2.2.4 Biological Activity Assay; 2.3 Results and Discussion; 2.3.1 Synthesis and Characterization of Peptide I; 2.3.2 Synthesis and Characterization of Peptide II; 2.3.3 Structure-Activity Relationship Studies; 2.4 Conclusion; References; 3 Protein Ligands Engineering; 3.1 Introduction; 3.2 Experimental Section; 3.2.1 Plasmid Construction. 3.2.2 Protein Expression and Purification3.2.3 Peptide Synthesis, Purification, and Characterization; 3.2.4 Preparation of TIP-1-MCherry Dimer; 3.2.5 Preparation of Water-Soluble QDs; 3.2.6 Agarose Gel Electrophoresis; 3.3 Results and Discussion; 3.3.1 A TIP1 Fusion Protein and Its Dimer as QD Ligands; 3.3.2 Tetrameric Proteins with Different Spatial Distribution of QD-Binding Sites; 3.3.3 Structural Transition of a Nanobelt Protein Ligand; 3.4 Conclusion; Appendix 3.1 Plasmid Information of pET21a-TIP1-MC; Appendix 3.2 Plasmid Information of pET21a-ULD-MCS. Appendix 3.3 Plasmid Information of pET21a-MC-NBAppendix 3.4 Mass Spectrum of the Peptide; Appendix 3.5 SDS-PAGE Results of the Proteins; Appendix 3.6 SDS-PAGE Results of Nanobelt-mCherry; References; 4 Coiled-Coil Binding-Induced Covalent Cross-Linking; 4.1 Introduction; 4.2 Experimental Section; 4.2.1 Peptide Synthesis; 4.2.2 Peptide Purification and Characterization; 4.2.3 Construction of pET28m-EGFP-CCE-1 Plasmid; 4.2.4 Expression and Purification of EGFP-CCE-1 Proteins; 4.2.5 Fitting the Cross-Linking Reaction to Second-Order Kinetics; 4.2.6 Peptide Cross-Linking and Kinetics Measurement. 4.2.7 In Vitro Protein Labeling and Kinetics Measurement4.3 Results and Discussion; 4.3.1 Crosslinking Reaction on the Latter Face; 4.3.2 Crosslinking Reaction in the Hydrophobic Core; 4.3.3 Multi-component Labelings; 4.3.4 Covalent Labeling of a Target Protein; 4.4 Conclusion; Appendix 4.1 List of the Synthetic Peptides and Their Molecular Weights; Appendix 4.2 Plasmid Information of pET28m-EGFP-CCE-1; References; 5 Cell Surface Receptor Labeling; 5.1 Introduction; 5.2 Experimental Section; 5.2.1 Construction of B2R Plasmids; 5.2.2 Construction of EGFR and hIP Plasmids.
• Publisher Details: Berlin, Germany : Springer
• Publication Date: 2016
• Extent: 1 online resource (xiii, 96 pages), illustrations (some color)
• Subjects: 572/.65; Peptides; Bioconjugates; SCIENCE -- Life Sciences -- Biochemistry; Bioconjugates; Peptides; Chemistry; Biotechnology; Protein Science; Nanotechnology; Bioorganic Chemistry; Peptides; Electronic books
• Languages: English
• ISBNs: 9783662533994; 3662533995; 3662533979; 9783662533970
• Related ISBNs: 9783662533970
• Notes: Note: Includes bibliographical references.; Note: Online resource; title from PDF title page (SpringerLink, viewed September 28, 2016).
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.