Opening a Can of Worm(‐like Micelle)s: The Effect of Temperature of Solutions of Functionalized Dipeptides

Abstract

A simple heat/cool cycle can be used to significantly affect the properties of a solution of a low‐molecular‐weight gelator at high pH. The viscosity and extensional viscosity are increased markedly, leading to materials with very different properties than when the native solution is used.

Synthesis of a Bis‐Urea Dimer and Its Effects on the Physical Properties of an Amphiphilic Tris‐Urea Supramolecular Hydrogel

“…The concentration of the NaOH solution affected the viscosity, which decreased with increasing NaOH concentration. (Figure S1) . Addition of hydrochloric acid to this solution instantly afforded a supramolecular hydrogel, which could be quantitatively analyzed in terms of its viscoelastic properties using a rheometer, and was found to be sufficiently stiff .…”

Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix

“…Moreover,t he formation of stable b-sheets in amyloid fibrils is related to the occurrence of some neurodegenerative diseases such as Alzheimer or Parkinson. [5] Actually,m any attempts have been made to explore the conversion from b-sheet to a-helix structure in several approaches.T hrough specific switching elements,s tructural rearrangements can take place in amyloid fibrils with b-sheet pattern. [4] Considering these facts,i ti ss peculated that modulating secondary structure transitions from b-sheet to a-helix cannot only serve as an effective strategy for the therapy of neurological diseases through the inhibition of b-sheet aggregation, but also extend the application of a-helix fibrils in drug delivery and controlled release,t hree-dimensional (3D) cell culture,tissue engineering and so on.…”

“…[4] Considering these facts,i ti ss peculated that modulating secondary structure transitions from b-sheet to a-helix cannot only serve as an effective strategy for the therapy of neurological diseases through the inhibition of b-sheet aggregation, but also extend the application of a-helix fibrils in drug delivery and controlled release,t hree-dimensional (3D) cell culture,tissue engineering and so on. [5] Actually,m any attempts have been made to explore the conversion from b-sheet to a-helix structure in several approaches.T hrough specific switching elements,s tructural rearrangements can take place in amyloid fibrils with b-sheet pattern. [6] Moreover,c omplementary interactions can drive helical folding within a-helical coiled coil peptides.…”

Engineering Biocompatible Scaffolds through the Design of Elastin‐Based Short Peptides

“…Short peptides are a class of low‐molecular‐weight gelators which have recently attracted attention for their scalability and modular nature . The library of amino acids available for synthesizing short peptides (typically 2–8 amino acids long) results in hundreds of potential gelators.…”

“…[17,18] Short peptides are ac lass of low-molecular-weight gelators which have recently attracted attention for their scalability and modular nature. [19][20][21][22] The library of amino acids available for synthesizing short peptides (typically 2-8 amino acids long) results in hundreds of potentialg elators. The ability to tune peptide properties such as charge,p K a ,a nd hydrophobicity by changing either the amino acid sequence or N-terminal capping group of the peptide has resulted in the generation of many promisingm aterials for cell culture, drug delivery,a nd tissue engineering.…”