Self-Assembling Peptide Synthesis

Fig.1 Self-assembling peptides ^[1].

Self-assembling peptides have the ability to spontaneously organize into well-defined structures or networks without the need for external forces or templates. They have good biocompatibility and controllability, can form nanostructures such as particles, fibers and gels, and perform specific morphological functions. In addition, they also exhibit a high degree of structural order. Self-assembling peptides represent a promising class of biomaterials with a wide range of potential applications, making them a subject of ongoing research and development in the scientific community. Alfa Chemistry offers comprehensive self-assembling peptide synthesis services, tailored to meet the specific needs of our clients. We have a team of experienced researchers who specialize in designing and synthesizing self-assembling peptides with precise control over their structure, composition, and functionality.

What We Offer

We specialize in providing self-assembling peptide synthesis services. Our services include:

Types Of Self-Assembling Peptides We Synthesize

The types of self-assembling peptides we can synthesize include but are not limited to the following:

• Amyloid-like peptides. Amyloid-like peptides are a type of self-assembling peptides that can form β-sheet structures. They usually have highly ordered secondary structures and are biologically linked to some neurodegenerative diseases such as Alzheimer's disease.
• β-Oligopeptides. β-Oligopeptides are a type of short peptide chain composed of β-amino acid residues. They are able to form self-assembled structures through hydration, often forming fibrous or micelle-like aggregates.
• Helical peptides. Helical peptides are a type of self-assembling peptides that can form helical structures. They usually stabilize the secondary structure through hydrogen bonding interactions, forming fibrous or membrane-like self-assemblies.

• Micelle-forming peptides. This type of peptides can form micelle structures in an aqueous environment, in which hydrophobic residues are gathered in the core and hydrophilic residues face the aqueous phase.
• Hydrogel-forming peptides. Hydrogel-forming peptides can self-assemble in an aqueous environment to form gel-like structures. Such peptides often have excellent biocompatibility and biodegradability and are used in tissue engineering and biomedical applications.
• Covalently cross-linked peptides. Covalently cross-linked peptides are a special type of self-assembling peptides that are cross-linked by covalent bonds to form a stable structure. These peptides often contain specific amino acid sequences that allow the assembly of well-defined nanostructures such as nanotubes, nanofibers, or hydrogels.

• Artificial Proteins. We can design artificial proteins by synthesizing specific amino acid sequences. These artificial proteins have specific self-assembly properties and can be used in fields such as nanotechnology, drug delivery, and biomaterials.
• Ion-complementary peptides. Ion-complementary peptides are characterized by alternating arrangements of hydrophilic and hydrophobic amino acid residues that self-assemble through electrostatic interactions, hydrogen bonds, and van der Waals forces.
• Surfactant-like peptides. Surfactant-like peptides are divided into hydrophilic and hydrophobic regions. The hydrophilic region is generally composed of 1 to 2 charged amino acid residues, and the hydrophobic region is generally composed of 3 to 9 non-polar amino acids.

Service Process