Designing phenylalanine-based hybrid biological materials: Controlling morphology: Via molecular composition

Srinivas Mushnoori, Kassandra Schmidt, Vikas Nanda, Meenakshi Dutt

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Harnessing the self-assembly of peptide sequences has demonstrated great promise in the domain of creating high precision shape-tunable biomaterials. The unique properties of peptides allow for a building block approach to material design. In this study, self-assembly of mixed systems encompassing two peptide sequences with identical hydrophobic regions and distinct polar segments is investigated. The two peptide sequences are diphenylalanine and phenylalanine-asparagine-phenylalanine. The study examines the impact of molecular composition (namely, the total peptide concentration and the relative tripeptide concentration) on the morphology of the self-assembled hybrid biological material. We report a rich polymorphism in the assemblies of these peptides and explain the relationship between the peptide sequence, concentration and the morphology of the supramolecular assembly.

Original languageEnglish (US)
Pages (from-to)2499-2507
Number of pages9
JournalOrganic and Biomolecular Chemistry
Volume16
Issue number14
DOIs
StatePublished - 2018
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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