China
Africa
Explore chapters and articles related to this topic
Applications of Marine Biochemical Pathways to Develop Bioactive and Functional Products
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Toni-Ann Benjamin, Imran Ahmad, Muhammad Bilal Sadiq
Collagen is a common fibrous protein found in all connective tissues (i.e., skin, bones, ligaments, tendons, and cartilage). The most abundant, cost-effective, and eco-friendly source of the bioactive compound is available as marine collagen obtained through marine waste streams (Cheung & Li-Chan, 2016; Suleria et al., 2015). Seafood processing by-products contain a rich content of functional molecules, such as proteins, bioactive peptides, collagen, polyunsaturated fatty acids, chitin, and fat-soluble vitamins (Lucarini et al., 2020). Collagen is characterized by a triple-helix structure made by three crosslinked alpha-amino acid chains, consisting of two homologous α1-chains and one α2-chain (Lionetto & Esposito Corcione, 2021). Gelatin is a protein derived from the partial hydrolysis of native collagen followed by thermal treatment. Further enzymatic hydrolysis can be used to extract collagen peptides from gelatin (Lionetto & Esposito Corcione, 2021).
Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Fibrous or fibrillar proteins are filiform, long and physically tough. They are mainly of animal origin and are insoluble in all common solvents such as water, acid, alkali solution and organic solvents. Fibrous proteins have structural and protective functions. The fibrous proteins are extremely strong and possess the elastomer characteristics. It is a heterogeneous group and includes the keratins and the proteins of connective tissues found in bones, skin, hair, nails, horns, hoofs, wool, and silk (36, 47). The important examples are: collagens, elastins, keratins, and fibroins. Collagens and their analogs elastins are the proteins of connective tissues, skin, cornea of the eyes, tendons, cartilages, and ligaments. They are also called ‘cellular glue’ as they help give tissues their shape and keep them strong, and are the major proteins of white connective tissues (tendons, cartilage) and of bone. Due to its abundance, strength and its directly proportional relation with skin aging, collagen has gained great interest in the cosmetic industry (51). Elastin has the additional property of being elastic as a rubber band (47). Keratins are rich in cystine, a sulfur amino acid, and are the major components of skin, hair, feathers, hoofs, nails, and horns (47). Fibroins are mainly composed of amino acids; glycine, alanine, and serine and are found in the fibers of silk (47). Fibrin is the protein formed when blood clots.
Proteins for Conditioning Hair and Skin
Published in Randy Schueller, Perry Romanowski, Conditioning Agents for Hair and Skin, 2020
Fibrous proteins (protein chains arranged in parallel) include the water-swellable (but not soluble) structural proteins keratin, collagen, and elastin, major components of hair, skin, and connective tissue, respectively. Intermolecular crosslinks are common in these proteins, particularly those containing the monomer cysteine (R = -CH2-SH). When oxidized, two cysteines form one cystine linkage (-CH2-S-S-CH2-). Such bonds are responsible for hair's strength as well as its ability to be reconfigured, or "permanent waved."
Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions
Published in mAbs, 2023
Seyed Farzad Baniahmad, Romane Oliverio, Ines Obregon-Gomez, Alma Robert, Anne E.G. Lenferink, Elena Pazos, Nick Virgilio, Xavier Banquy, Gregory De Crescenzo, Yves Durocher
Affinity peptides are versatile tunable tools that can be easily expressed as tags on recombinant proteins. This strategy ensures the efficient tagging of the protein since no extra conjugation step is required and removes the need for an additional purification step. Coiled-coil peptides are commonly used affinity systems derived from the coiled-coil structure, which is one of the most abundant naturally occurring motifs for protein folding and assembly.17 Structurally, this oligomerization motif consists of two or more α helices wrapped around each other. It is commonly found in many proteins involved in cellular activities, including transcription, muscle contractions, or viral fusion mechanisms.23–25 The fingerprint of this structure is a repeat of a seven-residue motif (heptad), the number of which can vary from 200 in naturally occurring fibrous proteins to only two heptads in a de novo designed synthetic coiled-coil.26 The E/K coiled coil is a de-novo-designed coiled-coil in which the Ecoil and Kcoil peptides, heptads: EVSALKE (Ecoil) and KVSALEK (Kcoil), form a highly specific, heterodimeric coiled-coil interaction with a high affinity, shown to be sufficiently strong in physiological conditions.27,28
Glaucoma – ‘A Stiff Eye in a Stiff Body’
Published in Current Eye Research, 2023
Sarah Powell, Mustapha Irnaten, Colm O’Brien
At a cellular level, the ECM plays a critical role in aging, stiffness and their downstream pathological consequences. Biologically, stiffness is defined as the ability of a tissue to resist deformation.62 The ECM, an extremely complex yet highly organized structure under constant tight regulatory control, provides a great deal of support-both biochemically and biomechanically- to cellular tissues and also acts as a substrate for cellular processes such as adhesion, differentiation and migration.63 The ECM is fundamentally composed of water, an array of fibrous proteins including collagen, vitronectin and fibronectin, proteoglycans, glycosaminoglycans and polysaccharides.64 Under normal circumstances, dynamic remodeling of ECM following cellular insult or injury functions as a protective cellular mechanism, one that restores tissue function and integrity. The level of ECM stiffness thus plays a central effector role in cellular behaviour.63,65
Proteomic analysis of pancreatic ductal adenocarcinoma
Published in Expert Review of Proteomics, 2020
Paula Meleady, Rozana Abdul Rahman, Michael Henry, Michael Moriarty, Martin Clynes
PDAC is one of the most stroma-rich cancers, which accounts for 50–80% of the tumor volume. The PDAC stroma supports tumor growth and promotes metastasis; it simultaneously serves as a physical barrier to drug delivery, and is highly resistant to conventional therapies. Activated pancreatic stellate cells (PSCs)/proliferating myofibroblasts are responsible for the production of stromal collagen of the extracellular matrix (ECM) including type 1 collagen and hyaluronic acid, and its function is influenced by pancreatic cancer cells [9]. Other ECM components include fibrous proteins like collagens, laminin and fibronectin and non-collagenous proteins like glycoproteins, proteoglycans and glycosaminoglycans. The ECM also contains components thought to influence stromal-cancer cell interactions, including growth factors, osteopontin, periostin, and serine protein acidic and rich in cysteine (SPARC). The cellular components of the stroma includes immune cells such as lymphocytes, macrophages, mast cells and myeloid derived suppressor cells along with vascular and neural elements (endothelial cells and neurons) [10].