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Engineering Retro-Proteins Highlights Immunoglobulin-Domain Scaffold Plasticity as a Framework for Therapeutic Discovery

Author

Listed:
  • André Hurtado
  • Israel Davila Aleman
  • Amber Gonda

    (Department of Cell Biology and Physiology, Brigham Young University, Provo, Utah, USA)

  • Christopher Mendoza

    (College of Business MBA program, California State University Chico, USA)

  • Mason Terry
  • Dario Mizrachi

    (Noorda College of Osteopathic medicine, Provo, Utah, USA)

Abstract

Amino acid sequences of native proteins are generally not palindromic. The protein molecule obtained as a result of reading the amino acid sequence backwards, i.e., a retro-protein, has the same amino acid composition and the same hydrophobicity profile as the native sequence, but may behave as a different molecule.

Suggested Citation

  • André Hurtado & Israel Davila Aleman & Amber Gonda & Christopher Mendoza & Mason Terry & Dario Mizrachi, 2026. "Engineering Retro-Proteins Highlights Immunoglobulin-Domain Scaffold Plasticity as a Framework for Therapeutic Discovery," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 64(4), pages 56746-56757, February.
    • Handle: RePEc:abf:journl:v:64:y:2026:i:4:p:56746-56757
    DOI: 10.26717/BJSTR.2026.64.010079
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    JEL classification:

    • R00 - Urban, Rural, Regional, Real Estate, and Transportation Economics - - General - - - General
    • Z0 - Other Special Topics - - General

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