Biopeptek’s HydroFobic Peptide is based on our proprietary platform technology that provides you custom peptide, hydrophobic peptides for your research needs.
What is the HydroFobic Peptide technology?
Biopeptek’s HydroFobic Technology includes:
- Hybrid Synthesis Platform: Solid Phase peptide synthesis (SPPS)/ Liquid Phase Peptide Synthesis (LPPS) technology, ligation technology and fragmentation technology.
- Combined Purification Platform:
- Gel Permeation Chromatography (GPC)
- Ion Exchange Chromatography (IEC)
- Reversed Phase High Performance Liquid chromatography (RP-HPLC)
HydroFobic Peptide technology improves synthesis efficiency in SPPS using coupling additives such as racemization suppressants, chotropic salts, beta-sheet disrupters, and alternative solvents. The following diagram describes the synthesis process.
Why is the HydroFobic Peptide technology developed?
The 3D structure, and consequently bioactivity, of individual proteins is largely determined by the primary sequence of its component amino acids. This inherent propensity of peptide chains to form ordered structures is the principle cause of the highly sequence specific variability in synthetic efficiency encountered during peptide assembly. As the peptide is elongated, it can form secondary structure or aggregates either with other peptide chains or with the polymer support, which can result in lower reaction rates. The effects can range from just a subtle slowing down to a complete failure of both deprotection and acylation reaction. In such extreme cases, the peptide has effectively become insoluble and is no longer available for reaction. The ease of assembly of a given sequence is generally hard to predict and is one of the factors that makes peptide synthesis interesting and challenging, although peptide containing stretches of contiguous hydrophobic amino acids like Ala, Val, Ile as well as those containing amino acids which can form intra-chain hydrogen bonds, such as Gln, and Thr, are frequently difficult to make. For this reason, it is generally better to adopt from outset synthetic strategies that mitigate the effect of structure formation, rather than trying to second guess which peptides may be problematic or wasting time and resources repeating failed syntheses. For this reason, Biopeptek developed HydroFobic Peptide technology that solves most of the synthesis problems.
What peptides are difficult to synthesize?
| Description | Explanation |
|---|---|
| Multiple Aspartic Acids (D) | Multiple Aspartic Acids (D) in a sequence frequently result in the formation of aspartimide adducts, resulting in a product of lower purity. |
| Adjacent Serines (S) | Adjacent Serines (-AA-S-) in a sequence frequently result in product that is low in purity and/or contain many deletions |
| Poly(GGGG) | Multiple consecutive Glycines (G) (4 or more) tend to undergo hydrogen bonding (gel formation) in the peptide backbone. The hydrogen bonding may cause difficulty in dissolving and purifying the peptide |
| Difficult amino acids: C, M, W | Especially in summer, it’s easily to oxidation if peptide containing C or M or W |
| >75% hydrophobic residues, and contains 25% charged residues | May be insoluble or only partially soluble in aqueous solutions |
| >50% hydrophobic residues, and contains 25% negative charged residues | May be insoluble or only partially soluble in aqueous solutions |
| >50% to 75% hydrophobic residues and without charged residues | May be insoluble or only partially soluble in aqueous solutions |
| Very hydrophobic peptides containing >75% hydrophobic residues | Generally not dissolve in aqueous solutions |
| Secondary Structure: The peptide containing streches of contiguous hydrophobic amino acids: Val, Ile, Ala as well as those containing amino acids wich can form intra-chain or inter-chain hydrogen bonds, such as Gln or Thr. | During synthesis, ?-sheet formation causes incomplete solvation of the growing peptide and results in a high degree of deletion sequences in the final product. |
