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PDA (Pentadeca Arginate)
PDA (Pentadeca Arginate)

PDA (Pentadeca Arginate)

$196.00 USD

PDA (Pentadeca Arginate) is a synthetic arginine-rich peptide complex studied for its potential role in cellular delivery systems, nitric oxide–related signaling, and membrane permeability. Composed of a sequence of arginine residues, PDA is investigated in laboratory settings for its ability to facilitate intracellular transport and interact with cellular membranes, making it relevant in peptide delivery and transport research.

In experimental models, arginine-rich peptides like PDA are explored for their potential to support nitric oxide pathways, vascular signaling, and cellular uptake mechanisms. Suggested research applications include investigations into transmembrane transport, endothelial function, cellular communication, and peptide-assisted delivery of biomolecules.

Its strong positive charge and affinity for negatively charged cell membranes allow PDA to be utilized in studies examining how peptides can enhance intracellular penetration and molecular trafficking, particularly in complex biological environments.
Milligrams

PDA (Pentadeca Arginate) is a poly-arginine peptide composed of approximately fifteen arginine residues, placing it within a class of molecules commonly referred to as cell-penetrating peptides (CPPs). These peptides are characterized by their high cationic charge density, which allows them to interact with negatively charged components of the cell membrane, including phospholipids and glycosaminoglycans.

One of the primary areas of research involving PDA is its role in cellular uptake and intracellular delivery. Studies on poly-arginine peptides (such as R8, R9, and longer arginine chains) have demonstrated their ability to translocate across cellular membranes via mechanisms including endocytosis and direct membrane penetration. PDA, with its extended arginine chain, is of interest for investigating enhanced delivery efficiency of peptides, nucleic acids, and other macromolecules into cells.

In addition to its transport capabilities, PDA is studied in relation to nitric oxide (NO) signaling pathways. Arginine is a known precursor to nitric oxide, a key signaling molecule involved in vascular tone, endothelial function, and cellular communication. While PDA itself is not directly converted into nitric oxide in the same manner as free L-arginine, its high arginine content makes it relevant in research exploring arginine-associated signaling environments and vascular biology.

PDA is also examined for its interaction with cell membranes and biointerfaces. Its strong electrostatic interactions allow it to bind to membrane surfaces, making it useful in studies of membrane permeability, peptide–lipid interactions, and drug delivery systems. These properties are particularly relevant in the development of advanced delivery platforms, including nanoparticle conjugation and peptide-based carriers.

In tissue and vascular research, arginine-rich peptides have been evaluated for their ability to influence endothelial cell behavior, including cellular adhesion, migration, and response to oxidative stress. PDA’s structure makes it suitable for studying these processes in controlled experimental models.

Due to its stability and high solubility, PDA is also used in formulation research, where it may be combined with other peptides or biomolecules to enhance delivery efficiency and bioavailability in vitro and ex vivo systems.
Research & References:

Research on Pentadeca Arginate is closely tied to the broader field of cell-penetrating peptides (CPPs), particularly poly-arginine sequences. Early foundational studies demonstrated that arginine-rich peptides can efficiently cross cell membranes and deliver biologically active cargo into intracellular compartments. These findings established CPPs as a key area of interest in molecular delivery and therapeutic design.

Mechanistically, poly-arginine peptides interact with negatively charged cell surface molecules such as heparan sulfate proteoglycans, initiating uptake via endocytosis or direct translocation. Studies have shown that increasing the number of arginine residues enhances cellular uptake efficiency, with longer chains (such as those approximating PDA) demonstrating improved internalization compared to shorter sequences.

In cellular biology research, poly-arginine peptides have been used to deliver proteins, peptides, RNA, and DNA into cells, enabling investigations into gene expression, signaling pathways, and intracellular targeting. These delivery capabilities have positioned peptides like PDA as valuable tools in biotechnology and experimental therapeutics.

Research into nitric oxide–related pathways has also intersected with arginine-rich peptide studies. While PDA is not directly metabolized like free arginine, its structural composition allows researchers to examine localized arginine-rich environments and their influence on endothelial signaling, oxidative stress responses, and vascular biology.

Additionally, studies have explored the role of poly-arginine peptides in membrane dynamics, including pore formation, lipid reorganization, and transient membrane destabilization. These mechanisms are critical for understanding how large molecules can enter cells without causing permanent membrane damage.

Emerging research also investigates the use of arginine-rich peptides in combination with nanotechnology, where they are conjugated to nanoparticles or drug carriers to enhance cellular uptake and targeting efficiency.

Overall, PDA represents a specialized tool for studying intracellular delivery, membrane interaction, and arginine-related signaling processes. Its relevance spans multiple research domains, including molecular biology, drug delivery systems, vascular research, and cellular transport mechanisms.

Futaki, S. et al., “Arginine-rich peptides: an abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery.” Journal of Biological Chemistry.

https://www.jbc.org/article/S0021-9258(20)73187-0

Wender, P. A. et al., “The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters.” PNAS.

https://www.pnas.org/doi/10.1073/pnas.96.26.14968

Nakase, I. et al., “Cellular uptake of arginine-rich peptides: roles for macropinocytosis and actin rearrangement.” Molecular Therapy.

https://www.sciencedirect.com/science/article/pii/S1525001616304461