Cell penetrating peptides (CPPs) are a diverse class of short peptides that are able to cross cell membranes without compromising their structural and functional integrity and have been extensively studied for the delivery of bioactive molecules, therapeutic agents, and theranostic cargoes within the cellular environment. With decades of hands-on experience in peptide synthesis and research, CD Formulation has developed specific skills and expertise that enable it to produce CPPs of superior quality. Our broad range of synthetic strategies coupled with in-depth expertise enables us to consistently meet our customers' expectations in delivering specialized peptides on time and on budget.
CPPs, also known as protein transduction domains (PTDs), are short, positively charged peptides consisting of less than 40 amino acids. They can cross cell membranes and transport a wide range of compounds, such as siRNA, nucleic acids, small molecules, proteins, and cytotoxic drugs, bringing them into cells in the process. The vast majority of bioactive molecules must enter cells to exert their functions. The main features of CPPs are low cytotoxicity, uptake by a wide range of cell types, dose-dependent efficiency, and no restrictions on the size or type of cargo. CPPs have been successfully applied to deliver different types of drugs, nanoparticles, and liposomes for disease diagnosis and treatment.
Fig. 1 Assembly of complex cell-penetrating peptide (CPP) structures. (Reissmann S, et al., 2014)
At CD Formulation, our team of peptide synthesis experts has the expertise and specific skills to design and synthesize high-quality CPPs for a variety of applications based on your needs.
Our scientists are familiar with a variety of synthesis techniques, including solid-phase peptide synthesis (SPPS), liquid-phase peptide synthesis (LPPS), and chemo-enzymatic peptide synthesis (CEPS), allowing us to select the most appropriate technology to support each individual peptide synthesis project. At the same time, we strictly follow quality control standards to ensure that we provide you with high-purity, low-impurity peptide products.
Our CPP synthesis services include but are not limited to:
A limitation of most CPPs is their lack of cell or tissue selectivity, which limits their use in clinical development. To address this, our peptide experts design your own CPP using three different universal controlled delivery strategies listed below.
In addition to peptide synthesis capabilities, CD Formulation combines flexible GMP manufacturing facilities with cutting-edge peptide analytical knowledge to provide a full range of quality control testing services to accelerate the commercialization of your products, including:
Published Data
Technology: Synthesis of Cell Penetrating Peptide
Journal: Sci Rep.
IF: 3.93
Published: 2016
Results:
The author designed and synthesized 5 cationic peptides (1 – 5): FAM-β-Ala-(l-Arg-l-Arg-l-Pro)3-(Gly)3-NH2 (1), which contained an l -Pro residue; FAM-β-Ala-(l-Arg-l-Arg-l-ProNH2)3-(Gly)3-NH2 (2), which contained an l-ProNH2 residue bearing a side-chain amino group; and FAM-β-Ala-(l-Arg-l-Arg-l-ProGu)3-(Gly)3-NH2 (3), which had an l-ProGu residue bearing a side-chain guanidino group. Furthermore, FAM -β-Ala-(l-Arg)2-(l-ProGu)2-(l-Arg)4-l-ProGu-(Gly)3-NH2 (4) and FAM-β-Ala-(l-Arg)6-(l-ProGu)3-(Gly)3-NH2 (5) and investigated their cell-penetrating abilities. The results showed only peptide 3 having the side-chain guanidinyl l- ProGu exhibited a secondary structural change in cellular environment, and demonstrated greater cell-penetrating activity than other peptides during cellular permeability tests.
Fig. 2 Chemical structures and sequences of peptides 1–5. (Yamashita H, et al., 2016)
CD Formulation's CPP synthesis services are tailored to meet the specific needs of researchers and organizations seeking high-quality peptides for drug discovery, vaccine development, diagnostics, and other scientific endeavors. Please don't hesitate to contact us if you are interested in our services. We look forward to cooperating with you.
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