laminin 1 β1 peptide

laminin 1 β1 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-RYVVLPR-OH

H-Arg-Tyr-Val-Val-Leu-Pro-Arg-OH

7

95.84%

C₄₂H₇₁N₁₃O₉

902.09

Synthetic

Powder

RYVVLPR polypeptide, derived from laminin 1, is a bioactive short peptide with significant implications in biomedical research. It was used to functionalize the self-assembling peptide scaffold RAD16-I.
This peptide is soluble in water at 10mg/ml (1% w/v) and forms hydrogels with nanofiber structures, exhibiting β -sheet conformation. In human aortic endothelial cell (HAEC) culture, it promotes cell adhesion with nearly 100% attachment rate, sustains HAEC phenotype, and accelerates the formation of confluent monolayers with enhanced cell growth compared to the unmodified scaffold. HAEC on this peptide-modified scaffold can release nitric oxide and deposit basement membrane components like laminin 1 and collagen IV, suggesting its potential in tissue engineering, drug screening, and cancer biology research for mimicking cell microenvironment and modulating cell behavior.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Skubitz AP, McCarthy JB, Zhao Q, Yi XY, Furcht LT. Definition of a sequence, RYVVLPR, within laminin peptide F-9 that mediates metastatic fibrosarcoma cell adhesion and spreading. Cancer Res. 1990 Dec 1;50(23):7612-22. PMID: 2253210.
• Genové E, Shen C, Zhang S, Semino CE. The effect of functionalized self-assembling peptide scaffolds on human aortic endothelial cell function. Biomaterials. 2005 Jun;26(16):3341-51. doi: 10.1016/j.biomaterials.2004.08.012. PMID: 15603830.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.