Post by skyship on Sept 28, 2011 14:55:17 GMT -5
I will stick to the idea that Morgellons is an extension of
Alzheimers, which is part of the process of Transhumanism.
When they found they could make nano out of amyloid like
material it would become the transformant. Oligomers are
the fibers, they are polymers. These monomers are made
of soy resin.....or the like.........vinyl or silica rubber like..Calcite, is in gall stones, is in kidney stones, is Bone morphogenic material. These
calcite, amyloids are in extracellular spaces, used as nano
replicators. Nanowires, are from M13 bacteriophage, sup35 and
sup45. The Evolutionary capacitors, found in heat shock proteins.
These wires are conducting. Recombinants used in head
of nanowire phage. Peptides, peptones, polypeptides, the
new name for these inorganic structures which form dimers,
oligomers, fibrils, protofibrils, the calcite is the bone forming
material, in extracellular spaces, junk dna, because it would
and could attach the quantum dots, the amphiphiles and
bolaamphiphiles. Oligomers.............. Oligo sugars......
the membrane proteins........
How it is done:
================================================
Nanomaterials: amyloids reflect their brighter side[/b]
Abstract
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine.
Keywords: Nanotechnology; self-assembly; peptide/protein; fibrils; tissue engineering; stem cells; drug delivery; nanowires
BEGINS with the MONOMER!
)Schematic representation of amyloid aggregation. The natively folded/unfolded monomeric form of protein slowly transforms to a partially folded intermediate and then gets converted to soluble oligomers and protofibrils. These oligomers eventually form β-sheet-rich fibrils. (B) Amyloid formation by nucleation dependent polymerization mechanism showing an initial lag phase and then elongation followed by a stationary phase. Preformed amyloid fibrils can acts as a ‘seed’ to accelerate the kinetics of fibril formation by reducing the lag time. Most of the functional and disease amyloid formation follow this mechanism. (C) Typical morphology of amyloid fibrils as observed under electron microscope.
www.nano-reviews.net/index.php/nano/article/viewFile/6032/8580/21579
clip:
Amyloid formation is generally considered as a ‘nucleation-dependent polymerization’ process (24, 25), where soluble native proteins are converted into aggregation-prone ‘partially folded intermediates’ that subsequently self-assemble into oligomers (nucleus) (Fig. 1B). These oligomers represent a heterogeneous population of different sized species and are highly dynamic in nature. Oligomers further proceed into mature fibrils in a very fast kinetics with monomer addition to the nuclei. Further, amyloid formation can be accelerated by the addition of ‘pre-formed nuclei’ (fibrils seed), which reduces the lag phase of nucleation (24).
Amyloid: a natural nanomaterial
Amyloids are highly organized fibrillar structures that hold great potential to be used as nanomaterials for various technological and biological applications (Table 1). The unique properties that make amyloid fibrils attractive for technological use include: (i) spontaneous formation of amyloids by (m)any protein/peptides under certain given conditions (17, 36, 37); (ii) stability, high mechanical stiffness comparable to silk and steel (2), and ability to form highly ordered structures (11); (iii) nucleation-dependent polymerization process, where preformed amyloid fibrils can act as seed to accelerate the kinetics of fibril formation (24); (iv) ability to tune physico-chemical properties of amyloid by modulation of amino acid sequences (38); (v) ease of functionalization of individual fibrils for specific applications (39). The functional group may be recruited at the amino acid side chain for applications such as receptor-ligand and gold-thiol interactions (8, 39); (vi) higher order amyloid aggregation of fibrils leading to formation of complex networks of filaments, gels and films (38, 40–42) that may be suitable for immobilizing enzymes, small molecules and drugs. Apart from these above-mentioned properties, amyloids display structural plasticity and their formation could be reversible depending upon the condition.
Now, compare to the created ones:
. Amyloid-like fibrils have been seen in a range of different shapes and forms including curly twisted fibrils, linear straight fibrils, rods, tapes and spherical clusters (such as spherulites) (40, 46–49). Tycko and coworkers have shown that two different modes of aggregation of Aβ40 lead to morphologically distinct amyloids with different secondary structure and toxicity (50). Recently, studies on the structure and intermolecular dynamics of amyloid fibrils by H/D exchange experiment revealed that monomers of amyloid fibrils are in continuous recycling within the fibrils (51). Amyloid fibrils assembly could also be reversed by changing conditions such as pH and dilution (20, 35, 38, 52).
The recycling behavior of amyloid fibrils may be exploited for specific applications. For example, the property of reversible self-assembly has been utilized in formulating long-acting drugs where controlled release of peptide molecule occurs from the fibril termini (38). Furthermore, the reversibility and structural plasticity could play important role in modulating the degradability of amyloid fibrils.
Peptide/protein self-assembly could also produce diverse set of biomaterials mimicking the extracellular matrix that can promote cell adhesion, migration and differentiation (54–56). Zhang and co-workers developed novel self-complementary β-sheet peptides using alternative positive and negative L-amino acids that could self-assemble under physiological conditions and form hydrogels (57–59) . These peptide fibrils were able to form extensive networks and support neuronal cell attachments, differentiation and extensive neurite outgrowth
Moreover, the scaffolds made by self-assembling peptides functionalized with different motifs (e.g. osteogenic growth peptide ALK in osteoblast tissue culture) served as excellent material for three-dimensional cell culture systems (61) (62). The peptide scaffolds promoted proliferation and osteogenic differentiation of mouse MC3T3-E1 cell, suggesting its application in bone tissue engineering (62). In addition, these materials were useful in vascularization, where it created a cellular milieu within the myocardium for survival and organization of endothelial cells (63). It was also reported that self-assembling peptide KLD-12 hydrogel provides an excellent scaffold for the production and accumulation of a cartilage-like ECM within 3D tissue culture that have application in cartilage tissue repair (55).
So, the Calcite that C. Carter talks of in video could be from these
AMyloid like creations, ......... so my article on the amyloids is
not far off, my friends. Meaning amyloid like was created to make
more amyloid, and was used for this new nanotech.......
The calcite is there, the gel is there, the morphological forms, the
nanowires, and is in the EXTRACELLULAR spaces, where the jnk dna
is.
=============================================
For review:
Shocking Connection between Chemtrails, Morgellons, and GMO – Experts Provide Proof
aircrap.org/shocking-connection-between-chemtrails-morgellons-gmo-experts-provide-proof/332294/
and C. Carters original:
aircrap.org/caroline-carter-speaks-about-morgellons-disease-heal/332261/
And my article on Amyloids:
Manna From Chemtrails: From amyloids to nanoids
morgspine.bravejournal.com/
=======================================
LETS GET TO THE BOTTOM OF THIS!
Skyship
=
Alzheimers, which is part of the process of Transhumanism.
When they found they could make nano out of amyloid like
material it would become the transformant. Oligomers are
the fibers, they are polymers. These monomers are made
of soy resin.....or the like.........vinyl or silica rubber like..Calcite, is in gall stones, is in kidney stones, is Bone morphogenic material. These
calcite, amyloids are in extracellular spaces, used as nano
replicators. Nanowires, are from M13 bacteriophage, sup35 and
sup45. The Evolutionary capacitors, found in heat shock proteins.
These wires are conducting. Recombinants used in head
of nanowire phage. Peptides, peptones, polypeptides, the
new name for these inorganic structures which form dimers,
oligomers, fibrils, protofibrils, the calcite is the bone forming
material, in extracellular spaces, junk dna, because it would
and could attach the quantum dots, the amphiphiles and
bolaamphiphiles. Oligomers.............. Oligo sugars......
the membrane proteins........
How it is done:
================================================
Nanomaterials: amyloids reflect their brighter side[/b]
Abstract
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine.
Keywords: Nanotechnology; self-assembly; peptide/protein; fibrils; tissue engineering; stem cells; drug delivery; nanowires
BEGINS with the MONOMER!
)Schematic representation of amyloid aggregation. The natively folded/unfolded monomeric form of protein slowly transforms to a partially folded intermediate and then gets converted to soluble oligomers and protofibrils. These oligomers eventually form β-sheet-rich fibrils. (B) Amyloid formation by nucleation dependent polymerization mechanism showing an initial lag phase and then elongation followed by a stationary phase. Preformed amyloid fibrils can acts as a ‘seed’ to accelerate the kinetics of fibril formation by reducing the lag time. Most of the functional and disease amyloid formation follow this mechanism. (C) Typical morphology of amyloid fibrils as observed under electron microscope.
www.nano-reviews.net/index.php/nano/article/viewFile/6032/8580/21579
clip:
Amyloid formation is generally considered as a ‘nucleation-dependent polymerization’ process (24, 25), where soluble native proteins are converted into aggregation-prone ‘partially folded intermediates’ that subsequently self-assemble into oligomers (nucleus) (Fig. 1B). These oligomers represent a heterogeneous population of different sized species and are highly dynamic in nature. Oligomers further proceed into mature fibrils in a very fast kinetics with monomer addition to the nuclei. Further, amyloid formation can be accelerated by the addition of ‘pre-formed nuclei’ (fibrils seed), which reduces the lag phase of nucleation (24).
Amyloid: a natural nanomaterial
Amyloids are highly organized fibrillar structures that hold great potential to be used as nanomaterials for various technological and biological applications (Table 1). The unique properties that make amyloid fibrils attractive for technological use include: (i) spontaneous formation of amyloids by (m)any protein/peptides under certain given conditions (17, 36, 37); (ii) stability, high mechanical stiffness comparable to silk and steel (2), and ability to form highly ordered structures (11); (iii) nucleation-dependent polymerization process, where preformed amyloid fibrils can act as seed to accelerate the kinetics of fibril formation (24); (iv) ability to tune physico-chemical properties of amyloid by modulation of amino acid sequences (38); (v) ease of functionalization of individual fibrils for specific applications (39). The functional group may be recruited at the amino acid side chain for applications such as receptor-ligand and gold-thiol interactions (8, 39); (vi) higher order amyloid aggregation of fibrils leading to formation of complex networks of filaments, gels and films (38, 40–42) that may be suitable for immobilizing enzymes, small molecules and drugs. Apart from these above-mentioned properties, amyloids display structural plasticity and their formation could be reversible depending upon the condition.
Now, compare to the created ones:
. Amyloid-like fibrils have been seen in a range of different shapes and forms including curly twisted fibrils, linear straight fibrils, rods, tapes and spherical clusters (such as spherulites) (40, 46–49). Tycko and coworkers have shown that two different modes of aggregation of Aβ40 lead to morphologically distinct amyloids with different secondary structure and toxicity (50). Recently, studies on the structure and intermolecular dynamics of amyloid fibrils by H/D exchange experiment revealed that monomers of amyloid fibrils are in continuous recycling within the fibrils (51). Amyloid fibrils assembly could also be reversed by changing conditions such as pH and dilution (20, 35, 38, 52).
The recycling behavior of amyloid fibrils may be exploited for specific applications. For example, the property of reversible self-assembly has been utilized in formulating long-acting drugs where controlled release of peptide molecule occurs from the fibril termini (38). Furthermore, the reversibility and structural plasticity could play important role in modulating the degradability of amyloid fibrils.
Peptide/protein self-assembly could also produce diverse set of biomaterials mimicking the extracellular matrix that can promote cell adhesion, migration and differentiation (54–56). Zhang and co-workers developed novel self-complementary β-sheet peptides using alternative positive and negative L-amino acids that could self-assemble under physiological conditions and form hydrogels (57–59) . These peptide fibrils were able to form extensive networks and support neuronal cell attachments, differentiation and extensive neurite outgrowth
Moreover, the scaffolds made by self-assembling peptides functionalized with different motifs (e.g. osteogenic growth peptide ALK in osteoblast tissue culture) served as excellent material for three-dimensional cell culture systems (61) (62). The peptide scaffolds promoted proliferation and osteogenic differentiation of mouse MC3T3-E1 cell, suggesting its application in bone tissue engineering (62). In addition, these materials were useful in vascularization, where it created a cellular milieu within the myocardium for survival and organization of endothelial cells (63). It was also reported that self-assembling peptide KLD-12 hydrogel provides an excellent scaffold for the production and accumulation of a cartilage-like ECM within 3D tissue culture that have application in cartilage tissue repair (55).
So, the Calcite that C. Carter talks of in video could be from these
AMyloid like creations, ......... so my article on the amyloids is
not far off, my friends. Meaning amyloid like was created to make
more amyloid, and was used for this new nanotech.......
The calcite is there, the gel is there, the morphological forms, the
nanowires, and is in the EXTRACELLULAR spaces, where the jnk dna
is.
=============================================
For review:
Shocking Connection between Chemtrails, Morgellons, and GMO – Experts Provide Proof
aircrap.org/shocking-connection-between-chemtrails-morgellons-gmo-experts-provide-proof/332294/
and C. Carters original:
aircrap.org/caroline-carter-speaks-about-morgellons-disease-heal/332261/
And my article on Amyloids:
Manna From Chemtrails: From amyloids to nanoids
morgspine.bravejournal.com/
=======================================
LETS GET TO THE BOTTOM OF THIS!
Skyship
=