Opioid Peptide Structures in Membranes: How Shape Determines Receptor Activation

NMR studies of opioid peptides in membrane environments revealed conformations distinct from solution structures, providing the actual receptor-interacting shapes needed for drug design.

Naito, Aira et al.·Current topics in medicinal chemistry·2004·Moderate EvidenceReview
RPEP-00953ReviewModerate Evidence2004RETHINKTHC RESEARCH DATABASErethinkthc.com/research

Quick Facts

Study Type
Review
Evidence
Moderate Evidence
Sample
Not reported

What This Study Found

Opioid peptide conformations in membrane-mimetic environments differed significantly from solution structures, revealing the biologically relevant receptor-interacting conformations for structure-based opioid drug design.

Key Numbers

How They Did This

review study on opioid-peptides, peptide-design.

Why This Research Matters

Relevant for opioid-peptides, peptide-design, receptor-signaling.

The Bigger Picture

Advances peptide/biomarker research.

What This Study Doesn't Tell Us

See abstract.

Questions This Raises

  • ?Further research needed.
  • ?Clinical translation to evaluate.

Trust & Context

Key Stat:
Key finding Opioid peptide conformations in membrane-mimetic environments differed significantly from solution structures, revealing the biologically relevant rec
Evidence Grade:
moderate evidence.
Study Age:
Published in 2004.
Original Title:
Conformational analysis of opioid peptides in the solid states and the membrane environments by NMR spectroscopy.
Published In:
Current topics in medicinal chemistry, 4(1), 135-45 (2004)
Database ID:
RPEP-00953

Evidence Hierarchy

Meta-Analysis / Systematic Review
Randomized Controlled Trial
Cohort / Case-Control
Cross-Sectional / ObservationalSnapshot without intervening
This study
Case Report / Animal Study

Summarizes existing research on a topic.

What do these levels mean? →

Frequently Asked Questions

What was studied?

Opioid Peptide Structures in Membranes: How Shape Determines Receptor Activation

What was found?

NMR studies of opioid peptides in membrane environments revealed conformations distinct from solution structures, providing the actual receptor-interacting shapes needed for drug design.

Read More on RethinkPeptides

Cite This Study

RPEP-00953·https://rethinkpeptides.com/research/RPEP-00953

APA

Naito, Aira; Nishimura, Katsuyuki. (2004). Conformational analysis of opioid peptides in the solid states and the membrane environments by NMR spectroscopy.. Current topics in medicinal chemistry, 4(1), 135-45.

MLA

Naito, Aira, et al. "Conformational analysis of opioid peptides in the solid states and the membrane environments by NMR spectroscopy.." Current topics in medicinal chemistry, 2004.

RethinkPeptides

RethinkPeptides Research Database. "Conformational analysis of opioid peptides in the solid stat..." RPEP-00953. Retrieved from https://rethinkpeptides.com/research/naito-2004-conformational-analysis-of-opioid

Access the Original Study

Study data sourced from PubMed, a service of the U.S. National Library of Medicine, National Institutes of Health.

This study breakdown was produced by the RethinkPeptides research team. We analyze and report published research findings without making health recommendations. All interpretations are based solely on the published abstract and study data.