Thermodynamic Characterization of Peptide Self-Assembly by Isothermal Titration Calorimetry (ITC) (CAT#: STEM-MB-2475-LGZ)

Introduction

Self-assembling peptides are an active area of biomedical research, perhaps due to the possibility of fine-tuning these molecules with respect to their final application. They can self-assemble into different types of nanostructures (fibers, micelles, tapes, cylinders, vesicles, etc.) through adopting various conformations (β-sheet, α-helix, β-hairpin, etc.). Different combinations of 20 amino acids, provided by nature, allow for the development of a broad range of peptide molecules with different properties. Some of these residues can influence the peptide structure in certain ways. For instance, proline (P) is known to be responsible for turns in β-hairpin structures as well as the beginning of α-helix strands, or cysteine (C) can promote cross-linking through disulfide bond formation.