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All pigmented proteins use aromatic amino acids and UV light

Discussion in 'Heal Your Hormones' started by Jack Kruse, Dec 22, 2015.

  1. Jack Kruse

    Jack Kruse Administrator

    Tyrosine is the base AA for all pigmented proteins.

    Another aromatic residue with non-negligible absorption in the near-UV region is tyrosine (Tyr-OH). At neutral pH tyrosine has absorption maxima at 220nm (є~9000 M-1cm-1) and 275nm (є~1400 M-1cm-1) (Creed, 1984a). At alkaline pH the OH group of tyrosine side chain deprotonates. The resulting tyrosinate (Tyr-O●−) has a slightly red-shifted absorption compared to tyrosine, with maxima at 240nm (є~11000 M-1cm-1) and 290nm (є~2300 M-1cm-1) (Creed, 1984a). Photoexcited tyrosine can fluoresce, decay non-radiatively, or undergo intersystem crossing to the triplet state, from which most of the photochemistry proceeds. Alternatively, at neutral pH, tyrosine can be photoionized through a biphotonic process that involves absorption of a second photon from the triplet state. This results in a solvated electron (e-aq) and a radical cation (Tyr-OH●+) that will rapidly deprotonate to create the neutral radical (Tyr-OH●). Photoionization of tyrosinate at high pH is monophotonic and results in a neutral radical (Tyr-O●) and a solvated electron (e-aq).

    Triplet state Tyr - OH +hv yields try-OH singlet +electron (e-eq)

    The triplet state tyrosine is rapidly quenched by molecular oxygen or nearby residues like tryptophan or disulphide bridges (Bent & Hayon, 1975b):

    An important photochemical mechanism in proteins involves reduction of disulfide bridges (SS) upon UV excitation of Trp and Tyr side chains (Kerwin & Rammele, 2007, Neves-Petersen et al., 2002 & 2009a). As shown above, UV-excitation of tryptophan or tyrosine can result in their photoionization and to the generation of solvated electrons (Bent & Hayon, 1975a & 1975b; Creed, 1984b, Kerwin & Rammele, 2007, Neves-Petersen et al., 2009a). The generated solvated electrons can subsequently undergo fast geminate recombination with their parent molecule, or they can be captured by electrophillic species like molecular oxygen, H3O+ (at low pH), and cystines (EE series of blogs on cysteine/cystine
     
  2. Jack Kruse

    Jack Kruse Administrator

    In the case where the electron is captured by the cystine, the result can also be the breakage of the disulfide bridge in proteins like glutathione. (Hoffman & Hayon, 1972)

    Here you begin to see how UV light and the aromatic AA begin to work to create all the pigmented proteins in our body. Activated electrons from UV is where the process begins.

    The resultant free thiol radicals/groups can then subsequently react with other free thiol groups to create a new disulfide bridge. Reduction of SS upon UV excitation of aromatic residues has been shown for proteins such as cutinase and lysozyme (Neves-Petersen et al., 2009a, 2006 & 2002), bovine serum albumin (Skovsen et al., 2009a; Parracino et al., 2011) prostate specific antigen (Parracino et al., 2010), and antibody Fab fragments (Duroux et al., 2007). As mentioned in the introduction, this phenomenon has led to a new technology for protein immobilization (LAMI, light assisted molecular immobilization) since the created thiol groups can bind thiol reactive surfaces leading to oriented covalent protein immobilization
     
    Antonis likes this.
  3. Jack Kruse

    Jack Kruse Administrator

    In the case where the electron is captured by the cystine, the result can also be the breakage of the disulfide bridge in proteins like glutathione. (Hoffman & Hayon, 1972)

    Here you begin to see how UV light and the aromatic AA begin to work to create all the pigmented proteins in our body. Activated electrons from UV is where the process begins.

    The resultant free thiol radicals/groups can then subsequently react with other free thiol groups to create a new disulfide bridge. Reduction of SS upon UV excitation of aromatic residues has been shown for proteins such as cutinase and lysozyme (Neves-Petersen et al., 2009a, 2006 & 2002), bovine serum albumin (Skovsen et al., 2009a; Parracino et al., 2011) prostate specific antigen (Parracino et al., 2010), and antibody Fab fragments (Duroux et al., 2007). As mentioned in the introduction, this phenomenon has led to a new technology for protein immobilization (LAMI, light assisted molecular immobilization) since the created thiol groups can bind thiol reactive surfaces leading to oriented covalent protein immobilization
     
    Antonis likes this.
  4. Jack Kruse

    Jack Kruse Administrator

    Pulsed UV illumination and the interaction of aromatic amino acids can halt activation of cancer cell membrane receptors (HER and EDGF) and thereby all downstream reactions that would lead to cancer, shutting down the cells’ biological functions. Moreover, there is new treatments based upon the ELF-UV release that cells use to activate the cell’s own cell death program. This has been documented on two human epidermal cancer cell lines (Olsen B.B. et al., 2007). The photonic dosage necessary for therapeutical results has additionally been determined. It turns out it is pretty low frequency as we saw in the Russian experiments and in Roeland van wijk's book.
     
    Joe Gavin likes this.
  5. Jack Kruse

    Jack Kruse Administrator

    This pathway is how cells use UV light to activate apoptosis pathways and prevents all cancers by deactivating disulfide bridges in CM proteins that use optical signaling. HOW?

    Throughout 4.5 billion year of molecular evolution, proteins have evolved in order to maintain the spatial proximity between aromatic residues (Trp, Tyr and Phe) and disulfide bridges (SS) (Petersen et al, 1999). There is a very special spatial geometry relationship that exists because of the interaction with the most powerful part of the solar spectrum of light (UV) measures the collisions. The aromatic amino acids become the first step in determining where the position and geometry of residues to act as nanosized antennas in the protein world that can capture UV light (from ~250-298nm). Once excited by UV light they can enter photochemical pathways likely to have harmful or beneficial effects on protein structures by affecting specific bonds like disulfide bonds in cysteine/cystine which are the most rare AA. It turns out cysteine/cystine disulfide bridges in proteins are excellent quenchers of the excited state of aromatic residues. This means they decrease the power present in UV light in excited aromatic amino acids. In this way they contributing this way to protein stability and activity, thereby affecting ubiquitin rates. UV light excitation of the aromatic residues is known to trigger electron ejection from their side chains (Bent & Hayon, 1975a; Bent & Hayon, 1975b; Bent & Hayon, 1975c; Creed, 1984a; Creed, 1984b; Kerwin & Rammele, 2007, Neves-Petersen et al., 2009a). These electrons can be captured by disulfide bridges in things like glutathione, leading to the formation of a transient disulfide electron adduct radical, which will dissociate leading to the formation of free thiol groups in the protein. This photochemical change leads to non optical signaling. Once disulfide bonds are broken we can inactive detrimental cell membrane receptors that cause epidermal cancers. The irony in all this.............UV prevents and doe snot cause cancer by these mechanisms. More irony for the skin and eye docs: This mechanism is now being used to develop drugs using nanotechnology and the ability of cells to make ELF-UV light.
     
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  6. Jack Kruse

    Jack Kruse Administrator

    Popularity is usually the path of idiocy. If 150 million oncologists say a foolish thing, it is still a foolish thing.
     
    nikita, Lahelada and Allin like this.

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