[D-Tyr6, ß-Ala11, Phe13, Nle14]-Bombesin (6-14)

Product Name: [D-Tyr6, ß-Ala11, Phe13, Nle14]-Bombesin (6-14)

Sequence One Letter Code: yQWAV-(ß-A)-HF-Nle-NH2

Sequence Three Letter Code: H-D-Tyr-Gln-Trp-Ala-Val-ß-Ala-His-Phe-Nle-NH2

Chemical Formula:C57H76N14O11

Molecular Weight: 1133.3

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: toad

Conjugation: Unconjugated

Code Nacres: NA.26

Application: [D-Tyr⁶, β-Ala¹¹, Phe¹³, Nle¹⁴]-Bombesin (6–14) is a synthetic bombesin analog engineered as a high-affinity ligand for the bombesin receptor family. The incorporated substitutions confer strong binding to all three bombesin receptor subtypes, enabling comprehensive receptor characterization and comparative signaling studies. This peptide is widely used in GPCR research, gastrointestinal hormone regulation studies, appetite signaling investigations, and cancer biology, particularly in models expressing gastrin-releasing peptide receptors.

Current Research: [D-Tyr⁶, β-Ala¹¹, Phe¹³, Nle¹⁴]-Bombesin (6–14) is a synthetic analog of the C-terminal bioactive region of bombesin, engineered to enhance receptor affinity, metabolic stability, and functional versatility. Bombesin peptides interact with the bombesin receptor family, which includes: GRPR (BB2; gastrin-releasing peptide receptor) NMBR (BB1; neuromedin B receptor) BRS-3 (BB3; bombesin receptor subtype 3) The incorporated substitutions—D-tyrosine at position 6, β-alanine at position 11, phenylalanine at position 13, and norleucine (Nle) at position 14—optimize receptor binding and broaden affinity across receptor subtypes. Structural and Functional Rationale The C-terminal region of bombesin (residues 6–14) contains the essential pharmacophore required for receptor activation. Specific modifications confer: D-Tyr⁶: Enhanced resistance to proteolytic degradation and improved receptor interaction stability β-Ala¹¹: Increased conformational flexibility and optimized receptor engagement Phe¹³ and Nle¹⁴: Enhanced hydrophobic interactions within receptor binding pockets These substitutions collectively produce a high-affinity ligand capable of engaging all three bombesin receptor subtypes, supporting comparative receptor studies. Biological Context Bombesin receptor activation triggers classical GPCR signaling pathways, typically involving: Gq-mediated phospholipase C activation IP₃ generation and intracellular Ca²⁺ mobilization PKC activation MAPK/ERK signaling cascades Physiologically, bombesin-related peptides regulate: Gastrointestinal hormone secretion Smooth muscle contraction Appetite and satiety signaling Neuroendocrine responses Overexpression of GRPR is observed in several cancers, including prostate, breast, and lung carcinomas, making bombesin analogs valuable in oncology research. Research Applications 1. GPCR Signaling and Pharmacology The analog is widely used to investigate receptor activation dynamics, ligand affinity, second messenger production, and receptor desensitization across bombesin receptor subtypes. 2. Gastrointestinal and Appetite Regulation Studies Bombesin peptides influence gut hormone secretion and satiety pathways. This analog supports mechanistic analysis of digestive and metabolic signaling. 3. Cancer Biology GRPR overexpression in tumors makes bombesin analogs important tools for studying: Tumor cell proliferation Receptor-mediated signaling Targeted imaging and therapeutic development 4. Comparative Receptor Profiling Because it binds all three bombesin receptor subtypes with high affinity, the peptide enables side-by-side evaluation of subtype-specific signaling responses. Experimental Considerations Receptor expression profiles should be confirmed in experimental systems to interpret signaling outcomes accurately. Dose–response analysis is recommended for precise characterization of potency and efficacy. Proteolytic stability and storage conditions should be optimized to maintain functional integrity.