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Updated: Aug 8, 2026

High-throughput Quantitative Real-time RT-PCR Assay for Determining Expression Profiles of Types I and III Interferon Subtypes
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Different stabilities of the N- and C- terminal domains of human interferon alpha

Z Skamlová1, E Kontseková, P Kontsek

  • 1Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovakia.

Immunological Investigations
|June 1, 1997
PubMed

Insights

Type I interferons (IFNs) have two independent polypeptide domains. The N-terminal domain of human interferon-alpha (IFN-alpha) is conformationally less stable and more flexible than the C-terminal domain, impacting receptor binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Type I interferons (IFNs) are crucial for immune responses.
  • Interferon-alpha (IFN-alpha) plays a key role in antiviral and antitumor activities.
  • Understanding the structural dynamics of IFN-alpha is essential for its therapeutic applications.

Purpose of the Study:

  • To investigate the structural independence of polypeptide domains in type I IFNs.
  • To analyze the differential molecular unfolding of human IFN-alpha domains during denaturation.
  • To correlate domain stability with IFN-alpha's receptor binding function.

Main Methods:

  • Utilized SDS (sodium dodecyl sulfate) solutions to induce protein denaturation.
  • Employed monoclonal antibodies (mAbs) to probe conformational changes in IFN-alpha.
  • Assessed the reactivity of mAbs with specific epitopes in N-terminal and C-terminal regions.

Main Results:

  • Confirmed the hypothesis of two structurally independent polypeptide domains in type I IFNs (regions 1-92 and 111-166).
  • Observed distinct molecular unfolding patterns between the N-terminal (residues 1-85) and C-terminal (residues 105-166) portions of human IFN-alpha.
  • Monoclonal antibodies detected significant changes in the N-terminal domain upon denaturation, but not in the C-terminal domain.

Conclusions:

  • The N-terminal domain of IFN-alpha exhibits lower conformational stability compared to the C-terminal domain.
  • This conformational flexibility in the N-terminal domain may be linked to its role in high-affinity receptor binding.
  • The findings support a model where functionally active sites possess greater conformational flexibility.

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