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CRYPTEINS

hidden peptides with biological activity

Crypteins are released by proteases or by radical coordination chemistry and photon capture and the transfer of energy into a peptide bond which leads to a cascade of energy events that have a spatial and temporal resolution that leads to the quantum entanglement of various molecules into structures that behave as a single entity when responding to the electromagnetism in the environment and the the creation of minimized energy states. 

The first cryptic peptide I identify was GAP573 from beta B2 crystallin protein that modulates gap junction communication through sequence homology to Cx43 and ZO PDZ2 domain. The sequence FHPSS having the ability to bind calcium. I used the enzyme elastase I to cleave the peptide off the protein beta B2 crystallin which resulted initially in a wide range of peptides being generated in the presence of calcium and the peptide that I was targeting precipitated out of solution. This resulted in the disappearance of the peptide when analyzed by RP HPLC analysis. So I tried the hydrolysis reaction in the absence of calcium and this resulted in a specific cleavage C-terminal to valine resulting in selective cleavage and release of the targeted peptide GAP573. I then used ultrafiltration to separate the enzyme and remaining protein from the peptide and then precipitate the peptide with calcium and combine it with alginate to produce the finished product (see above). 

The structural features of the peptide have been analyzed and in silico analysis has been performed to determine if it could interact with the target protein Cx43 and zona occludens PDZ2 domain. Looks like an unusual binding event occurs to prevent the interaction between these two proteins which provides a way for the mechanism of action. I also saw other features of the peptide being important for its function which is related to its ability to be phosphorylated on the penultimate serine residue and this switches off the peptide from being able to modulate gap junction communication.

The eye lens fiber cells are DNA free, and an immuno-privileged site due to tryptophan oxidation in the vitreous humor. DNA would cause opacity in the lens so the DNA is destroyed to produce the fiber cells and the fiber cells are filled with crystallin proteins.  The protein concentration is incredibly high within the lens fiber cells. It means protein isolation from this tissue is a practical approach to production of the peptides when elastase I is immobilized on resin and reused as part of the process. 


GAP573's ability to bind calcium and perform photon capture via the photoelectric effect means that one or many of the 27 isotopes of calcium are formed and each one of these has a specific half-life related to a frequency of operation (the atomic clock). It appears to be how high energy photons are generated within the lens fiber cells. The calcium isotopes with an imbalance between protons and neutrons perform a decay via beta minus process releasing photons of light and generating a new atom. Calcium 40 does K+ electron capture and Ca 41 does beta plus, whereas calcium 45 does beta minus. In beta plus you lose a proton to generate an atom one less than the initial atom. This would generate potassium. The normal levels of Na+ 20 micromol g-1, K+ 60 micromol g-1, Mg2+ 5.5 micromol g-1, and Ca2+ 0.1-0.5 micromol g-1.


The cataract lens has a higher concentration of potassium and calcium and a lower concentration of magnesium and sodium.  In a cataract lens they are Na+ 136.1 micromol g-1, K+ 9.33 micromol g-1, Mg2+ 3.6 micromol g-1, and Ca2+ 9.31 micromol g-1. Dilsiz et al., Cell Biochem Funct. 2000. 

Photon capture by coordination chemistry in the C-terminal extensions of crystallin proteins is responsible for the modulation of mineral concentration within the lens fiber cells through the capture of various frequencies of electromagnetism in the peptide structure. The small amount of scandium in the lens suggests a photon capture neutron generation and K+, beta minus, and beta plus cycle that involves scandium 44/21 which has a half-life of 3.97 hours. So processing of the lens in the presence and absence of photons that trigger this cycle will lead to an increase in photon capture and scandium production. But the form of scandium formed is unstable. The imbalance of the minerals in the lens of a cataract suggests that this cycle has been upset.

40/20 Ca --> K+ --> 41/20 Ca

41/20 Ca --> 42/20 Ca

42/20 Ca --> 43/20 Ca

43/20 Ca --> 44/20 Ca

44/20 Ca --> 45/20 Ca

45/20 Ca --> beta - --> 44/21 Sc

44/21 Sc --> beta + --> 43/20 Ca

K+ captures photons

beta plus reduces 1 proton and increases 1 neutron

beta minus increases 1 proton and decreases 1 neutron

So changes are due to isotope formation which is driven by photon capture. The UV light is captured by the aromatic ring of phenylalanine and is responsible for the photon capture and transfer of the energy into the coordinated calcium leading to the isotope energy cascade.

 
Ca fraunhofer 2_edited_edited.jpg

Fraunhofer lines

calcium

The H and K lines are prominent absorption lines in the spectra of stars like the Sun and cooler due to singly ionized calcium (Ca II). Named by Joseph von Fraunhofer, they occur in the near-ultraviolet at wavelengths of 3969 and 3934 Å, respectively (see Fraunhofer lines). Emission in the H and K lines is also common in some kinds of eruptive variables, such as flare stars and RS Canum Venaticorum stars.

 

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