Crystal Structure of Anti-Cancer Macrocyclic Peptide Bound to Its Target Reveals Drug Design Details

Crystal structures of a high-affinity macrocyclic peptide bound to the Grb2 SH2 cancer signaling domain revealed precise binding interactions, guiding further optimization of this anticancer peptide drug approach.

Phan, Jason et al.·Journal of molecular biology·2005·Preliminary Evidencein-vitro
RPEP-01074In VitroPreliminary Evidence2005RETHINKTHC RESEARCH DATABASErethinkthc.com/research

Quick Facts

Study Type
in-vitro
Evidence
Preliminary Evidence
Sample
Not reported

What This Study Found

X-ray crystal structures of a high-affinity macrocyclic peptide mimetic bound to Grb2 SH2 domain revealed specific hydrogen bonds and hydrophobic contacts driving picomolar binding — providing the structural blueprint for optimizing this cancer drug scaffold.

Key Numbers

How They Did This

in-vitro study on cyclic-peptides, cancer.

Why This Research Matters

Relevant for cyclic-peptides, cancer, peptide-design.

The Bigger Picture

Advances peptide research with clinical implications.

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 X-ray crystal structures of a high-affinity macrocyclic peptide mimetic bound to Grb2 SH2 domain revealed specific hydrogen bonds and hydrophobic cont
Evidence Grade:
preliminary evidence.
Study Age:
Published in 2005.
Original Title:
Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain.
Published In:
Journal of molecular biology, 353(1), 104-15 (2005)
Database ID:
RPEP-01074

Evidence Hierarchy

Meta-Analysis / Systematic Review
Randomized Controlled Trial
Cohort / Case-Control
Cross-Sectional / ObservationalSnapshot without intervening
This study
Case Report / Animal Study
What do these levels mean? →

Frequently Asked Questions

What was studied?

Crystal Structure of Anti-Cancer Macrocyclic Peptide Bound to Its Target Reveals Drug Design Details

What was found?

Crystal structures of a high-affinity macrocyclic peptide bound to the Grb2 SH2 cancer signaling domain revealed precise binding interactions, guiding further optimization of this anticancer peptide drug approach.

Read More on RethinkPeptides

Cite This Study

RPEP-01074·https://rethinkpeptides.com/research/RPEP-01074

APA

Phan, Jason; Shi, Zhen-Dan; Burke, Terrence R; Waugh, David S. (2005). Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain.. Journal of molecular biology, 353(1), 104-15.

MLA

Phan, Jason, et al. "Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain.." Journal of molecular biology, 2005.

RethinkPeptides

RethinkPeptides Research Database. "Crystal structures of a high-affinity macrocyclic peptide mi..." RPEP-01074. Retrieved from https://rethinkpeptides.com/research/phan-2005-crystal-structures-of-a

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.