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60 results about "Random coil" patented technology

A random coil is a polymer conformation where the monomer subunits are oriented randomly while still being bonded to adjacent units. It is not one specific shape, but a statistical distribution of shapes for all the chains in a population of macromolecules. The conformation's name is derived from the idea that, in the absence of specific, stabilizing interactions, a polymer backbone will "sample" all possible conformations randomly. Many linear, unbranched homopolymers — in solution, or above their melting temperatures — assume (approximate) random coils. Even copolymers with monomers of unequal length will distribute in random coils if the subunits lack any specific interactions. The parts of branched polymers may also assume random coils.

Modified type-I collagen, modification method, and collagen gel prepared from modified type-I collagen

InactiveCN110343169AReduced triple helixControllable viscoelasticityConnective tissue peptidesPeptide preparation methodsFiberBiological materials
The invention belongs to the field of medical biological materials, and particularly discloses a modified type-I collagen, a modification method, and collagen gel prepared from the modified type-I collagen. The modification method comprises the steps of (1) uniformly mixing weak acid with a type-I collagen at the temperature of 2-10 DEG C to prepare an acid collagen solution; (2) utilizing a phosphate buffering solution for dialysing the acid collagen solution to obtain a neutral collagen solution; (3) removing bubbles in the neutral collagen solution; (4) utilizing a rotational rheometer forcutting the neutral collagen solution after bubble removal under a liquid seal condition, and conducting standing after cutting to prepare the modified type-I collagen. According to the modified type-I collagen, the modification method, and the collagen gel prepared from the modified type-I collagen, the collagen is modified through mechanical cutting. The method is simple and efficient, three-helix structures of collagen molecules can be reduced on the basis that other substances do not need to be introduced, and random coil structures are added, so that fibers of the assembled collagen are controllable in diameter, pore and viscoelasticity.
Owner:WUHAN POLYTECHNIC UNIVERSITY

Spandex fiber with reversible shape memory effect, and preparation method and application thereof

The invention discloses a spandex fiber with a shape memory effect and a preparation method of the spandex fiber. The spandex fiber is prepared from the following components: a crystalline polyether or polyester diol monomer, a diisocyanate monomer, a polyurethane chain extender, a polyurethane cross-linking agent and a peroxide initiator. The spandex material has a double cross-linking structure, the first cross-linking structure is a cross-linking network formed by the polyurethane cross-linking agent, and the second cross-linking agent is polyurethane secondary cross-linking initiated by decomposition of the peroxide initiator; when the temperature is higher than a melting temperature of a soft section of the fiber, an oriented crystal area in the fiber is shrunk into a random coil state due to crystallization melting, and the fiber length is shortened, so that a second cross-linking network is compressed; when the temperature of the fiber is lower than a crystallization melting temperature of the spandex, molten soft segment molecular chains in the fiber are subjected to oriented crystallization again under the action of tensile stress provided by the compressed second recross-linked network in the system, and it is shown that the length of the fiber is increased; and the above process has the characteristics of repeatability and reversibility along with the change of temperature.
Owner:WUYI UNIV

Preparation and application of novel Arcainflata Reeve oxidation-resistant active peptide

The invention relates separation preparation and application of an Arcainflata Reeve oxidation-resistant active peptide. The separation preparation method comprises the following steps: peeling and cleaning Arcainflata Reeve, carrying out tissue homogenization, carrying out hydrolysis technique screening and optimization, centrifugating, taking the supernate, and carrying out freeze-drying to obtain an active polypeptide component; and sequentially carrying out ultrafiltration interception concentration, ion-exchange chromatography, gel filtration and high-efficiency exclusion chromatography on the active component to finally obtain the oxidation-resistant active polypeptide with the purity of 99%. Multiple modern protein purification techniques are creatively utilized to separate the active polypeptide with definite material basis from Arcainflata Reeve hydrolysate; the molecular weight of the active polypeptide is 17578.31Da; and the active polypeptide contains the following secondary structures: 40.8% of alpha-spiral, 24.7% of beta-fold, 15.9% of beta-corner and 18.6% of random coil. The polypeptide has obvious oxidation-resistant activity; the in-vitro removal DPPH, ABTS and hydroxy free radical IC50 values are respectively 3.89, 0.22 and 10.77 mg/ml; and the polypeptide can prolong the average life of the Caenorhabditis elegans by 18.29%. Therefore, the active peptide can be used for development and application of antioxidants, medicinal cosmetics or health products.
Owner:于荣敏
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