Structural analysis reveals gelation and amphipathic crystal packing in heterochiral isoleucine dipeptides, highlighting mechanisms of peptide self-assembly.
Key Points
To examine the supramolecular behavior and self-assembly properties of heterochiral aliphatic d-Ile-l-Xaa dipeptides across various solvent conditions.
Assessed the gelation capacity of d-Ile-l-Xaa dipeptides (where Xaa represents Ala, Val, Leu, or Ile) in organic solvents and neutral pH buffered water.
Tracked the transition of metastable dipeptide gels into crystalline structures.
Analyzed molecular arrangement and packing modes using single-crystal X-ray diffraction.
Heterochiral d-Ile-l-Xaa dipeptides formed metastable gels across tested solvent systems and neutral pH buffer.
The metastable gels underwent rapid transitions into crystalline phases suitable for structural characterization.
X-ray diffraction revealed that the molecules organize into distinct amphipathic layers.