A capped dipeptide which simultaneously exhibits gelation and crystallization behavior

Adam D. Martin, Jonathan P. Wojciechowski, Mohan M. Bhadbhade, Pall Thordarson

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Short peptides capped at their N-terminus are often highly efficient gelators, yet notoriously difficult to crystallize. This is due to strong unidirectional interactions within fibers, resulting in structure propagation only along one direction. Here, we synthesize the N-capped dipeptide, benzimidazole-diphenylalanine, which forms both hydrogels and single crystals. Even more remarkably, we show using atomic force microscopy the coexistence of these two distinct phases. We then use powder X-ray diffraction to investigate whether the single crystal structure can be extrapolated to the molecular arrangement within the hydrogel. The results suggest parallel β-sheet arrangement as the dominant structural motif, challenging existing models for gelation of short peptides, and providing new directions for the future rational design of short peptide gelators.
Original languageEnglish
Pages (from-to)2245-2250
Number of pages6
JournalLangmuir
Volume32
Issue number9
DOIs
Publication statusPublished - 8 Mar 2016
Externally publishedYes

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