Lipidation Alters the Structure and Hydration of Myristoylated Intrinsically Disordered Proteins

Jingjing Ji, Md Shahadat Hossain, Emily N. Krueger, Zhe Zhang, Shivangi Nangia, Britnie Carpentier, Mae Martel, Shikha Nangia, Davoud Mozhdehi

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Lipidated proteins are an emerging class of hybrid biomaterials that can integrate the functional capabilities of proteins into precisely engineered nano-biomaterials with potential applications in biotechnology, nanoscience, and biomedical engineering. For instance, fatty-acid-modified elastin-like polypeptides (FAMEs) combine the hierarchical assembly of lipids with the thermoresponsive character of elastin-like polypeptides (ELPs) to form nanocarriers with emergent temperature-dependent structural (shape or size) characteristics. Here, we report the biophysical underpinnings of thermoresponsive behavior of FAMEs using computational nanoscopy, spectroscopy, scattering, and microscopy. This integrated approach revealed that temperature and molecular syntax alter the structure, contact, and hydration of lipid, lipidation site, and protein, aligning with the changes in the nanomorphology of FAMEs. These findings enable a better understanding of the biophysical consequence of lipidation in biology and the rational design of the biomaterials and therapeutics that rival the exquisite hierarchy and capabilities of biological systems.

Original languageEnglish (US)
Pages (from-to)1244-1257
Number of pages14
JournalBiomacromolecules
Volume24
Issue number3
DOIs
StatePublished - Mar 13 2023

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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