Dermorphin | CAS /

Product Details

CasNo： /

Molecular Formula： C40H50N8O10

Product Overview

Dermorphin, CAS 77614-16-5, is a naturally occurring heptapeptide with the amino acid sequence Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2.

The peptide is structurally notable for two features: a D-alanine residue at position 2 (D-Ala²) and a C-terminal amide. These characteristics distinguish Dermorphin from many conventional short peptides composed entirely of L-amino acids.

Dermorphin has been widely studied as a peptide ligand in mu-opioid receptor (MOR / OPRM1) research and as a model for investigating peptide–receptor recognition, stereochemistry, and structure–activity relationships.

Basic Information

Item	Information
Product Name	Dermorphin
CAS No.	77614-16-5
Molecular Formula	C40H50N8O10
Molecular Weight	Approx. 802.9 g/mol
Peptide Length	7 amino acids
Sequence	Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2
Key Structural Feature	D-Ala²
C-Terminus	Amidated (-NH2)
Peptide Type	Heptapeptide / Opioid Peptide
Research Target	Mu-opioid receptor (MOR / OPRM1)

Structural Features

D-Alanine at Position 2

One of the most distinctive features of Dermorphin is the presence of D-alanine at the second residue.

Most naturally occurring peptides are composed predominantly of L-amino acids. The presence of a D-amino acid makes Dermorphin a useful molecular model for studying how stereochemistry can influence peptide conformation, receptor recognition, and ligand–receptor interactions.

C-Terminal Amidation

Dermorphin terminates in Ser-NH2, giving the peptide a defined C-terminal amide.

C-terminal amidation is an important structural feature in many biologically active peptides and can influence molecular charge, conformation, receptor interaction, and analytical behavior.

Compact Seven-Residue Sequence

Although Dermorphin contains only seven amino acids, its combination of D-amino-acid stereochemistry and terminal amidation gives the peptide a distinctive molecular profile.

Its defined sequence also makes it suitable as a reference structure in comparative studies of short peptide analogs and modified peptide sequences.

Research Background

Mu-Opioid Receptor Research

Dermorphin has been extensively investigated in relation to the mu-opioid receptor (MOR), encoded by the OPRM1 gene.

Research involving Dermorphin has contributed to the understanding of:

• Peptide–receptor recognition
• Ligand binding selectivity
• Receptor pharmacology
• Short-peptide conformational behavior
• Amino-acid stereochemistry in receptor interaction

These studies are generally conducted using receptor-binding assays, cellular models, biochemical systems, or other controlled research platforms.

Peptide–Receptor Interaction Studies

The short and well-defined sequence of Dermorphin provides a useful model for studying how individual amino-acid residues contribute to receptor recognition.

Particular attention is often given to the influence of D-Ala², aromatic residues, and terminal amidation on peptide conformation and receptor interaction.

Structure–Activity Relationship Research

Dermorphin has also been used as a reference peptide in structure–activity relationship (SAR) studies.

Research may compare:

• D- versus L-amino-acid substitutions
• Individual residue replacements
• Sequence truncation
• Terminal modifications
• Related peptide analogs

Such studies help clarify the relationship between peptide structure, stereochemistry, and receptor recognition.

Analytical and Structural Characterization

Dermorphin can be characterized using standard peptide analytical techniques.

Common research methods include:

• High-performance liquid chromatography (HPLC)
• Mass spectrometry (MS)
• LC-MS analysis
• Molecular-weight verification
• Sequence confirmation
• Terminal-modification analysis

Because Dermorphin contains a D-amino-acid residue and a C-terminal amide, analytical interpretation should consider both the amino-acid sequence and the defined terminal structure.

Frequently Asked Questions

What makes Dermorphin structurally unusual?

Dermorphin contains D-alanine at position 2, while most naturally occurring peptide sequences are dominated by L-amino acids. It also has a C-terminal amide.

How many amino acids are present in Dermorphin?

Dermorphin is a seven-amino-acid peptide, or heptapeptide.

What is the amino acid sequence of Dermorphin?

The sequence is:

Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2

Which receptor is commonly studied with Dermorphin?

Dermorphin is most commonly associated with research involving the mu-opioid receptor (MOR / OPRM1).

Why is D-Ala² important in Dermorphin research?

The D-configuration at position 2 provides a useful model for studying how amino-acid stereochemistry influences peptide conformation and receptor recognition.

Which analytical techniques are commonly used to characterize Dermorphin?

HPLC, MS, LC-MS, molecular-weight verification, and sequence-related analyses are commonly used in peptide characterization research.

This page is provided for scientific and informational purposes only.