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PT-141 (bremelanotide) is a synthetic cyclic heptapeptide analogue of α-melanocyte-stimulating hormone (α-MSH) that acts as an agonist at melanocortin receptors, including MC3R and MC4R.
Bremelanotide is the chemical name for PT-141, a synthetic cyclic heptapeptide analog derived from melanocortin peptide research. It differs from analogs of α-melanocyte-stimulating hormone (α-MSH) in that it has a conformationally controlled cyclic peptide backbone with a D-phenylalanine residue and norleucine substitution.
The peptide has a molecular formula of C50H68N14O10 and has a molecular weight of approximately 1025.18 g/mol. Its cyclic structure distinguishes it from linear melanocortin sequences and has been investigated in relation to peptide conformation, receptor-binding characteristics and resistance to enzymatic degradation.
PT-141 is recognized in laboratory research principally as a melanocortin receptor ligand. Experimental studies have used the compound to investigate ligand–receptor interactions, melanocortin receptor pharmacology, structure–activity relationships and receptor-mediated signaling. Its defined molecular structure also permits characterization using analytical techniques including high-performance liquid chromatography (HPLC) and mass spectrometry.
PT-141 is a conformationally constrained cyclic peptide constructed from seven amino-acid residues. Its sequence is commonly represented as Ac-Nle-c[Asp-His-D-Phe-Arg-Trp-Lys]-OH, with cyclization occurring between the aspartic acid and lysine residues. This intramolecular linkage restricts conformational flexibility compared with corresponding linear peptide structures.
Several additional structural features distinguish PT-141 from naturally occurring melanocortin sequences. These include N-terminal acetylation, incorporation of norleucine and the presence of D-phenylalanine. The use of a D-amino acid and cyclization are established peptide-design approaches for modifying conformational behavior and susceptibility to enzymatic degradation.
PT-141 has a combination of hydrophilic and hydrophobic structural areas due to its polar and nonpolar amino acid side chains. Its charge properties under various experimental settings are also influenced by ionizable residues, especially arginine and histidine.
PT-141 has been investigated primarily as a melanocortin receptor ligand. The melanocortin receptor family consists of five G-protein-coupled receptor subtypes, designated MC1R through MC5R. Experimental pharmacology has examined the interaction of cyclic melanocortin analogs with these receptor systems to characterize ligand affinity, receptor selectivity and downstream molecular signaling.
Published experimental studies describe PT-141 as having activity at several melanocortin receptor subtypes, with MC3R and MC4R representing important targets in its pharmacological characterization. Research involving melanocortin ligands has therefore used receptor-expression systems, binding experiments and functional assays to examine the molecular interactions associated with these receptors.
Melanocortin receptors of the G-protein-coupled receptor (GPCR) type are the most prevalent. Studies of receptor activation often investigate coupling to intracellular signaling pathways, such as those involving adenylyl cyclase and cyclic adenosine monophosphate (cAMP). These precise signaling systems suggest measurable experimental results for receptor–ligand interaction research.
The cyclic configuration of PT-141 is also relevant to structure–activity research. Conformational restriction can alter the spatial orientation of amino-acid side chains involved in receptor recognition. The presence of D-phenylalanine, norleucine and N-terminal acetylation provides additional structural variables that have been examined within melanocortin peptide chemistry.
Consequently, PT-141 provides a defined synthetic molecule for experimental investigation of melanocortin receptor pharmacology, peptide–receptor recognition, GPCR signaling and peptide structure–activity relationships.
This summary reflects findings reported in published preclinical and in vitro research. The original studies supporting this information are listed in the references.
PT-141 has been examined in experimental studies involving melanocortin receptors. Research in this area includes receptor-binding characterisation, ligand selectivity and comparison of synthetic melanocortin sequences across different receptor subtypes.
Signaling mechanisms linked to melanocortin receptor activation have been studied in lab settings. These investigations offer experimental models for describing GPCR-associated signaling and the molecular processes that take place after ligand-receptor contact.
The cyclic structure of PT-141 makes it relevant to structure–activity relationship research. Investigations can compare structural characteristics such as cyclisation, amino-acid substitutions, stereochemistry and conformational restriction with the molecular behaviour of related melanocortin peptides.
Melanocortin ligand interactions with particular receptor subtypes have been demonstrated using experimental receptor systems. PT-141 can be quantitatively compared with structurally similar peptide analogs using binding affinity and functional receptor assays.
Additionally, PT-141's amino acid composition, cyclic architecture, molecular mass, chromatographic performance, and stability under specific experimental settings have all been studied from the standpoint of peptide chemistry.
Solid-phase peptide synthesis (SPPS), which enables the sequential integration of the necessary amino acid residues followed by the proper cyclization and terminal modification procedures, can be used to create synthetic PT-141. The target peptide can then be separated from synthesis-related contaminants and shortened sequences by purifying crude synthesized material.
Peptide-related contaminants can be found in a sample and chromatographic purity can be evaluated using analytical high-performance liquid chromatography (HPLC). It is possible to confirm molecular mass and offer proof of chemical identity using liquid chromatography–mass spectrometry (LC–MS) or similar mass-spectrometric methods.
Additional analytical procedures may be employed where required to investigate composition or structural characteristics.
Batch-specific analytical results should be documented through a Certificate of Analysis (CoA) containing the relevant batch or lot number, compound identity, testing date, analytical method and measured purity. Analytical documentation should correspond specifically to the batch of research material supplied.
The lyophilized research material PT-141 should be stored in a controlled setting with little exposure to light, heat, or moisture. Unopened lyophilized material is usually stored in a frozen or refrigerated laboratory according to the supplier's confirmed requirements and batch documentation.
The physical stability of lyophilized peptide material may be impacted by frequent exposure to air humidity; hence containers should be kept tightly covered and shielded from moisture. Additionally, frequent freeze-thaw cycles and needless temperature changes should be avoided.
Where material is reconstituted for analytical laboratory work, an appropriate laboratory-grade solvent should be selected according to the requirements of the experimental method. Prepared solutions may exhibit different stability characteristics from lyophilised material and should therefore be handled according to validated laboratory procedures.
Bremelanotide, a synthetic cyclic heptapeptide that is a member of the melanocortin peptide analog class, is frequently referred to by the scientific designation PT-141. Research on melanocortin receptors and peptide chemistry have examined its specified cyclic structure.
Yes. PT-141 is a synthetic cyclic heptapeptide, meaning its structure contains seven amino-acid residues arranged within a conformationally constrained peptide architecture.
Published experimental research has characterised PT-141 in relation to the melanocortin receptor family. MC3R and MC4R are among the receptor subtypes examined in molecular and pharmacological studies involving the compound.
Cyclisation constrains the peptide backbone and alters its three-dimensional conformational behaviour compared with a corresponding linear peptide. Cyclic peptide structures are frequently investigated in structure–activity and peptide-stability research.
The molecular weight of bremelanotide is approximately 1025.18 g/mol, based on its molecular formula of C50H68N14O10.
PT-141 can be characterized using analytical techniques such as LC-MS and HPLC. HPLC certification provides information on chromatographic purity, whereas mass spectrometry can be used to verify molecular mass and determine identity.
For research and laboratory use only. Not for human or animal consumption.
PT-141 is supplied exclusively as a research material for qualified laboratory and analytical applications. Product information is provided solely for chemical, scientific and technical reference and is not intended to provide instructions concerning administration, dosing, diagnosis, treatment or prevention of any disease or condition.
