NATURAL POLYMERS MU SCI 13 2018 1 NATURAL POLYMERS 4 Proteins’ Fibres III ELASTIN Dr. Ladislav Pospíšil 29716@mail.muni.cz January 2018/13 Where is ELASTIN found in the Human Body? •Great amount of the ELASTIN is found in the Blood Vessel near to the Heart, further in the Ligaments, in the Skin and in the Tendons. •Elastin is the not soluble Scleroprotein, its Name is derived from its elastic Properties •Scleroprotein is the Denomination for the any Protein having approximately the fibrilar Shape •Scleroprotein are Water insoluble and e.g. Elastin, Keratin and Fibroin belong to this Group January 2018/13 NATURAL POLYMERS MU SCI 13 2018 2 What is the Difference between ELASTIN and COLLAGEN •COLLAGEN is the crystalline a helix, creating whole Hierarchy of Structures from the primary > secondary > tertiary > quaternary •ELASTIN is AMORPHOUS CROSSLINKED Scleroprotein, which does not creating Helixes (neither a no b) neither b Sheets January 2018/13 NATURAL POLYMERS MU SCI 13 2018 3 ELASTIN – the primary Structure 1 •Composition of the ELASTIN is rich in Amino acids, especially in GLYCINE, ALANINE, PROLINE, VALINE and LEUCINE. •ELASTIN contains also relatively many basic Lysine's Rests and ELASTIN has therefore Isoelectric Point lower than 10. January 2018/13 NATURAL POLYMERS MU SCI 13 2018 4 LYSIN (Lys, K) Amminoacido_lisina_formula.png ELASTIN – primary Structure 2 January 2018/13 NATURAL POLYMERS MU SCI 13 2018 5 Amino acids’ Composition of the TROPOELASTIN The Number of the Particular Amino acids the Molecule Asparagine 2 Proline 87 Leucine 37 Hydroxyproline 9 Glycine 267 Thyrosine 13 Serine 8 Alanine 174 Phenylalanine 22 Glutamine 15 Valine 97 Lysine 38 Threonine 11 Isoleucine 15 Arginine 6 ELASTIN – primary Structure 3 January 2018/13 NATURAL POLYMERS MU SCI 13 2018 6 Two Sequences LAAALAAL or LAALAAAL are necessary for the Creating the Bond between the ELASTIN Molecules of the ELASTIN ATTENTION! The right one Letter Marking for the LYSINE (K) is not used here! The RIGHT MARKING IS: Lysine K, and not L! L is the RIGHT MARKING for LEUCIN ELASTIN Molecule is created of approx. 400 Amino acids Sequences which are able to create the Bonds between the ELASTIN Molecules are separated by approx. 150 Amino acids Approx. 400 Amino acids + GGVIG---LAALAAAL---LAALAAAL----------------LAALAAAL---G----- > 150 < Amino acids Marking of the Amino acids in this Sequence above: G – Glycine, V – Valine, I – Isoleucine, L – Lysine, A - Alanine January 2018/13 NATURAL POLYMERS MU SCI 13 2018 7 Biogenic Amino acids Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V) Proline (Pro, P) Leucine (Leu, L) Amminoacido_glicina_formula.png Amminoacido_alanina_formula.png Amminoacido_valina_formula.png 800px-Amminoacido_prolina_formula_svg.png Amminoacido_leucina_formula.png January 2018/13 NATURAL POLYMERS MU SCI 13 2018 8 A biogenic amine is a biogenic substance with one or more amine groups. They are basic nitrogenous compounds formed mainly by decarboxylation of amino acids or by amination and transamination of aldehydes and ketones. Biogenic amines are organic bases with low molecular weight and are synthesized by microbial, vegetable and animal metabolisms. In food and beverages they are formed by the enzymes of raw material or are generated by microbial decarboxylation of amino acids Importance in food Biogenic amines can be found in all foods containing proteins or free amino acids and are found in a wide range of food products including fish products, meat products, dairy products, wine, beer, vegetables, fruits, nuts and chocolate. In non-fermented foods the presence of biogenic amines is mostly undesired and can be used as indication for microbial spoilage. In fermented foods, one can expect the presence of many kinds of microorganisms, some of them being capable of producing biogenic amines. They play an important role as source of nitrogen and precursor for the synthesis of hormones, alkaloids, nucleic acids, proteins, amines and food aroma components. However, food containing high amounts of biogenic amines may have toxicological effects. What is creating the Crosslinking in the ELASTIN January 2018/13 NATURAL POLYMERS MU SCI 13 2018 9 TROPOLELASTIN keeps partially its GLOBULAR STRUCTURE ELASTIN has after Crosslinking mainly the FIBRILAR STRUCTURE already ELASTIN 6.png Reversible Deformation of the ELASTIN January 2018/13 NATURAL POLYMERS MU SCI 13 2018 10 ELASTIN keeps partly its GLOBULAR STRUCTURE before Deformation ELASTIN has mainly the FIBRILAR STRUCTURE after the DEFORMATION ELASTIN 4.png ELASTIN is elastic in the HYDRATED STATE only, it is not so for the Dry ELASTIN ! Water acts as a LUBRICANT between the ELASTIN Molecules. It resembles VULCATISATION of the RUBBER! The RUBBER is also reversible crosslinked. What is the PRINCIPLE of the ELASTIN’S Elasticity •The smaller Molecules so called TROPOELASTIN are crosslinked by assistance of the ENZYMATIC CATALYSIS by the Desmosine and Isodesmosine Molecules • January 2018/13 NATURAL POLYMERS MU SCI 13 2018 11 300px-Desmosine_Structural_Formulae_V_1_svg.png 200px-Isodesmosine_svg.png Crosslinking is done via LYSINE in the ELASTIN Molecules, which create these Crosslinking Compounds What is creating the actual ELASTIC FIBRE January 2018/13 NATURAL POLYMERS MU SCI 13 2018 12 800px-2W86_(Fibrillin).png img911.jpg Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue. Fibrillin is a major component of the microfibrils that form a sheath surrounding the amorphous elastin. Fibrillin + Elastin ELASTIN in the Human Skin January 2018/13 NATURAL POLYMERS MU SCI 13 2018 13 ELASTIN 18.jpg ELASTIN 14.jpg ELASTIN 16.jpg ELASTIN 10.jpg ELASTIN in the Human Skin January 2018/13 NATURAL POLYMERS MU SCI 13 2018 14 ELASTIN 6.png ELASTIN 9.png The Skin growing old or the old Skin is not more able to create the elastic Fibres of the ELASTIN in the Human Skin already. These Fibres are cleaved by Enzyme ELASTASE. The Skin is loosing its Elasticity and the Wrinkles ate created …. COACERVATION •COACERVATION is the REVERSIBLE PROCESS, when the Secondary Structure of the Polymer Chain is changed •These changed Secondary Structures can then create by Aggregation the Reversible Tertiary Structures •These changed Structures are called COACERVATE January 2018/13 NATURAL POLYMERS MU SCI 13 2018 15 COACERVATION of the TROPOELASTINE January 2018/13 NATURAL POLYMERS MU SCI 13 2018 16 KOACERVACE ELASTINU imagesLFPVH872.jpg KOACERVACE ELASTINU imagesMHXJXL9A.jpg Tropoelastin aggregates at physiological temperature due to interactions between hydrophobic domains. This process is reversible and thermodynamically controlled. The Change of the Secondary Structure THESE PICTURES ILLUSTRATE THE TERMS „COACERVATION and COACERVATE „ ONLY. They are not related directly to ELASTIN. The Change of the TERTIARY STRUCTURE TROPOLELASTIN > ELASTIN > a ELASTIN January 2018/13 NATURAL POLYMERS MU SCI 13 2018 17 ELASTIN 6.png ELASTIN is very resistant from the chemical Point of Viiew. For Example, it is resistant to the short Time Action of the 80 % w/w H2SO4 or 4-N NaOH. The so called a ELASTIN (MW » 60000 - 80000) is Water soluble after partial Hydrolysis. The a ELASTIN can then associate by some Chain Sequences > COACERVATION b ELASTIN arises from the ELASTIN after the very intensive scission besides the a ELASTIN. COACERVATION does not occur for the b ELASTIN , probably its Molecules are too short (MW » 5000) and they are not rich enough of the Sequences able to form the Associates Standard ELASTIN is not able to do COACERVATION ELASTIN in the HIDE & LEATHER •The TECHNICAL IMPORTANCE of the ELASTIN is low in general •ELASTIN forms the smaller Part then the COLLAGEN in the Hide, occurring in the outer Part of the Hide and in the Under hide connective tissue •ELASTIN is resistant to the most technological Steps of the Hide Tannin to Leather, except for the enzymatic Bate •ELASTIN can contribute to the Leather Elasticity, abut there are not common View on this Phenomena. Some View exist, the ELASTIN should be removed during Tannin. •Analytical Monitoring of the ELASTIN after Tannin is based on the Determination of the VALINE after Hydrolysis of the Leather, because there are approx. 18 % w/w of the VALINE there (the highest Concentration in all the Proteins) January 2018there. NATURAL POLYMERS MU SCI 13 2018 18 The Importance of the ELASTIN in the Nutrition January 2018/13 NATURAL POLYMERS MU SCI 13 2018 19 •ELASTIN has the low Importance in the Nutrition due to its chemical and enzymatic Resistance, this Protein is hardly to be digest •ELASTIN must be cleaved by enzymatic or chemical partly cleaved if should be used the Animal Feed