Self-assembling Peptides

Myr5A peptide is an acylated peptide composed of apolipoprotein A1 (ApoA1) analog peptide 5A peptide coupled to the saturated fatty acid myristate. Myr5A peptide self-assembled into lipid nanostructures can be used to encapsulate anthracycline Doxorubicin (HY-15142A) and Valrubicin (HY-13772) for compound release studies in vitro.

Ac-IHIHIYI-NH2 is a fibrous heptapeptide that forms fibril-like structures with even higher esterase activity.

EAK16-II is an amphipathic peptide that inhibits the self-sorting of EAKIIH6 in a concentration-dependent manner.

H-Phe-Phe-Phe-Phe-Phe-OH has a self-assembled structure, which can be assembled into an ordered autofluorescent elongated structure, showing mechanochromic properties.

IEIK 13 is a self-assembling peptide (SAP) sequence. IEIK 13 can be used for the research of cartilage tissue engineering

RAD16-I (RADA16) is a non-directed self-assembling peptide hydrogel. Under physiological conditions, RAD16-I spontaneously forms a three-dimensional nanofiber network that mimics the extracellular matrix, and possesses excellent properties such as high water content, biocompatibility and degradability. RAD16-I serves as an ideal scaffold for three-dimensional cell culture. RAD16-I not only maintains cell viability and induces self-organization, but also supports cell adhesion, proliferation, differentiation and insulin secretion, effectively stabilizes islet clusters and promotes directed differentiation of the cardiac lineage. RAD16-I can construct a cell-friendly nano-microenvironment for research related to diseases such as myocardial infarction and diabetes.

FEFEFKFK is an octapeptide that self-assembles into fibrillar structures. FEFEFKFK is able to form gels at concentrations greater than about 7 mg/mL. The self-assembly and gelation properties of FEFEFKFK help to understand the mechanism of amyloid fibril formation in protein misfolding diseases such as Alzheimer's disease and Parkinson's disease.