LyP-1 peptide

LyP-1 peptide

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

H-CGNKRTRGC-OH

H-Cys-Gly-Asn-Lys-Arg-Thr-Arg-Gly-Cys-OH

9

95.2%

C₃₆H₆₅N₁₇O₁₂S₂

992.13

Synthetic

Powder

LyP-1 (CGNKRTRGC), a cyclic phage-displayed nonapeptide was identified as a tumor lymphatic vessel homing peptide. LyP-1 accumulated in the tumor lymphatics but not the tumor blood vessels of several tumor xenograft models including osteosarcomas, prostate and breast cancers, and metastatic lymph nodes of the vascular endothelial growth factor C (VEGF-C) overexpressing MDA-MB-435 tumors. In addition, LyP-1 recognizes the hypoxic tumor lesions. LyP-1 is a unique peptide due to its tumor penetrating ability and the inbuilt antitumor activity. LyP-1 was internalized and inhibited the MDA-MB-435 tumor cell growth in a dose dependent manner with an IC50 of approximately 66 uM. This effect was LyP-1 specific and no effect on cell viability was detected when cells were treated with the control peptides (CRVRTRSGC, CGEKRTRGC). Later the cell surface associated mitochondrial protein p32/gC1qR was identified as the LyP-1 interacting partner expressed by tumor cells and tumor-associated macrophages that are often incorporated into the walls of tumor lymphatic vessels. p32 is expressed in several tumor types as well as in atherosclerotic lesions. The LyP-1 peptide has been used in several applications for tumor targeted delivery of imaging and therapeutic agents. Timur et al. elucidated the interaction between LyP-1 and p32 by generating alanine scan derivatives of the LyP-1 peptide followed by interaction studies using molecular docking and Molecular Mechanics Poisson–Boltzmann Surface Area (MM–PBSA). The structureactivity relationship data generated by alanine-scan thermodynamics revealed 3Asn, 4Lys, 5Arg, and 7Arg as the most essential amino acids responsible for the p32 binding. The shortened variant of LyP-1 (truncated LyP-1; tLyP-1) with the highest tumor penetration activity conferred by its exposed CendR internalizing domain is reviewed under the tumor penetrating peptides.

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

• Zhang, L. et al. Canc. Res. 66, 5696 (2006); Akerman, M. et al. PNAS 99, 12617 (2002); Laakkonen, P.et al. Nat. Med. 8, 751 (2002).

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.