Dermorphin Powder CAS 77614-16-5

Dermorphin HAc Introduction

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Dermorphin Powder is a natural heptapeptide derived from the skin secretions of South American frogs. Its molecular formula is C40H50N8O10, with a molecular weight of approximately 802.87, and its CAS number is 77614-16-5. The core feature of this product lies in the presence of a rare D-type amino acid (D-Ala) in its sequence. This non-gene-encoded chiral structure makes it more stable in the body than ordinary L-type peptides and less prone to being degraded by proteases.

What is the function of Dermorphin Acetate?

Dermorphin Powder is a natural heptapeptide extracted from the skin of South American frogs and belongs to a highly selective μ-opioid receptor agonist. It can specifically bind and activate the μ-opioid receptors in the body. In the field of basic research, it is often used as a tool molecule to explore receptor functions, structure-activity relationships, and associated signaling pathways.
DERMORPHIN ACETATE has an extremely strong binding ability to μ receptors. This is because the peptide chain structure contains special D-type amino acids (D-Ala). Compared to conventional peptides, this structural feature makes the molecule more stable and less prone to being decomposed by protein enzymes in the body. Currently, the research focus is on structural modifications of various derivatives and analogues, attempting to create candidate molecules that can act through nasal or oral routes. The research aims to retain its excellent biological activity while improving the potential adverse effects related to opioid receptor agonism.

What are the unique characteristics of Dermorphin in biochemistry?

From a biochemical perspective, the unique advantages of this molecule are manifested in multiple aspects: The vast majority of natural polypeptides are composed of L-amino acids, while the second position of the Dermorphin Powder sequence contains D-alanine. This special chiral structure can stabilize the molecular conformation, enhance the ability to resist enzymatic degradation, and, compared to ordinary L-type polypeptides, is less likely to be decomposed in the biological fluid environment, effectively prolonging the duration of action. At the same time, DERMORPHIN ACETATE and specific endogenous receptors have extremely strong binding capabilities and subtype selectivity. Through precise matching, they become important research probes for exploring the spatial structure of receptors, the characteristics of binding regions, and the mechanism of signal transduction. In addition, this molecule is also often used as a basic template for studying the relationship between structure and function. Researchers replace different amino acids within the sequence to analyze the impact of each residue on the overall activity. Such basic research helps clarify the three-dimensional folding mode of polypeptides and the rules of interaction with targets, and has important reference value for understanding the mechanism of protein-ligand interaction.

MF of Dermorphin

CAS	77614-16-5
Molecular formula	C40H50N8O10
Molecular weight	802.87
EINECS	202-853-6
Melting point	157-159 °C
Density	1.363±0.06 g/cm3

Specification

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FAQ: 

Q1:How stable is the structure of Dermorphin?
Its stability is outstanding, and its unique chiral structure is the core biochemical feature of it.
Q2:What changes can type D amino acids bring about?
Changing the molecular chiral configuration makes the polypeptide less susceptible to protease degradation, thereby prolonging the molecule's retention time in the biological environment.
Q3:What role does the D-Ala in the sequence play?

The D-Alanine in the peptide chain can stabilize the molecular conformation and enhance the ability to resist protease degradation.

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