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Smart Polymeric Biomaterials in Tissue Engineering
Published in Rajesh K. Kesharwani, Raj K. Keservani, Anil K. Sharma, Tissue Engineering, 2022
Akhilesh Kumar Maurya, Nidhi Mishra
Silk fibroin is a natural biopolymer produced by Bombycoidea family of insect, that is, silkworms. Bombyx mori (B. mori) is the main source of silk that is produced by the Bombycidae family (Inoue et al., 2007). Basic structure of SF consists of alanine (Ala) (35%), glycine (Gly) (38%), and serine (Ser) (12%) (Herrera et al., 2017) (Figure 2.4). SF is a heterodimeric protein with a heavy (H) chain (~325 kDa) and a light (L) chain (~25 kDa) connected at Cys-172 of the L-chain and Cys c-20 of the H-chain by forming (Mondal et al., 2007). Polar amino acids, particularly tyrosine, valine, and acidic amino acids, are also present in the SF chain (Vepari and Kaplan, 2007). Fibrous protein of SF has been used for the formation of films, 3D scaffolds, and microspheres because of its excellent biostability, biocom-patibility, slow biodegradability, oxygen permeability, good mechanical properties, and minimal inflammatory and immunogenic response (Zuo et al., 2006; Numata and Kaplan, 2010; Nazarov et al., 2004).
Petroleum Geochemical Survey
Published in Muhammad Abdul Quddus, Petroleum Science and Technology, 2021
Proteins are of two types; one is fibrous and the other is globular. Fibrous proteins support and connect the tissues, muscles, skin and hair of the body. Fibrous proteins are comparatively stable and non-reactive. Globular proteins maintain and regulate the biological functions in living organisms. Another class of proteins contains a non-protein group as well in their molecular structure. The non-protein groups can be either carbohydrate (glucose) or lipid or nucleic acid or a metal ion. Accordingly proteins are named as carbohydrate-protein, lipo-protein, nucleo-protein and metallic-protein. Non-protein groups impart additional biological functions in the protein. Some proteins also act as catalysts. Such a protein is known as a catalytic enzyme. It catalyzes certain biological metabolism processes. Enzymes are more active and flexible than proteins.
Biomolecules
Published in Volodymyr Ivanov, Environmental Microbiology for Engineers, 2020
There are two types of tertiary structures: globular proteins (globe = sphere), which are usually water soluble, and fibrous proteins, which are insoluble in water. Self-folding in globular proteins is performed so that the hydrophobic parts of amino acids are directed toward the interior of the protein molecule, whereas the hydrophilic parts are bound outward, allowing dipole–dipole interactions with water molecules and ensuring the solubility of the protein molecule. The majority of globular proteins are enzymes, protein catalysts of biochemical reactions. Fibrous proteins form long protein filaments due to self-folding with the hydrophobic groups of amino acids directed outward, which ensures the insolubility of the molecule in water. Fibrous proteins perform structural functions in the cell or organism, connecting different parts and covering the organism.
Collagen-coated silk fibroin nanofibers with antioxidants for enhanced wound healing
Published in Journal of Biomaterials Science, Polymer Edition, 2023
Sowmya Selvaraj, Chandrasekar Inbasekar, Suryalakshmi Pandurangan, Nishad Fathima Nishter
Upon the skin damage owing to an acute or chronic injury, a multi-cascade event gets initiated for the contraction and closure of the wound and for the re-establishment of the skin’s barrier function, known as wound healing [1]. Wound dressings provide a favorable environment to facilitate the healing process [2]. Previous reports have shown that the wound dressing materials are prepared from a wide range of biocompatible materials viz., (alginates, gelatin, poly (caprolactone), poly (vinyl alcohol), cellulose and chitosan) in different forms like nanofibers, sponges, hydrogels, nonwoven fabrics, films and hydrocolloids [3]. Nanofibers are more desirable in wound management than the other structures due to their extracellular matrix-like architecture, large surface-to-volume ratio, which allows efficient cell attachment, and their high and interconnected porosity which facilitates the transport of oxygen and nutrients for cell growth. Both natural and synthetic polymers have been explored for the preparation of nanofibers. Among the natural polymers, fibrous proteins like collagen and silk fibroin play a significant role in skin tissue engineering, especially wound healing [4–6].
Moisture management and antimicrobial performance of collagen peptide enriched knitted fabrics
Published in The Journal of The Textile Institute, 2021
Ali Serkan Soydan, Gizem Karakan Günaydin, Haluk Ergezer, Sema Palamutcu
Apart from early researches, selection of collagen peptide based raw material as the component fibre of active wear fabric yarns might be useful due to its inherited features such as antimicrobial efficiency, and wound healing accelerating property beside its sustainable characteristic. Collagen is the most abundant animal protein, accounting for almost 30% of total protein in animal body. This fibrous protein plays an important role for providing the biological and structural integrity of extracellular matrix of the tissues in the body. In fishes, collagen is usually extracted out of meat, skin, fins, scale, and fish wastes. The extracted fish collagen can be purified for use in cosmetics, medical, sports, and nutrition, etc. Those collagen peptides have been discovered as one of the alternative antimicrobial sources as the potential health risks of synthetic antimicrobials have increased (Felician et al., 2018). Researchers have reported that almost all fish peptides have antibacterial or bacteriostatic functions against several gram-negative and -positive strains (Najafian & Babji, 2012; Rajanbabu & Chen, 2011).
The prevalence of urinary incontinence in nulliparous female sportswomen: A systematic review
Published in Journal of Sports Sciences, 2019
Sania Almousa, Alda Bandin Van Loon
A decrease in collagen in the pubovesical ligament has been linked to the development of UI (Keane, Sims, Abrams, & Bailey, 1997). It has been noticed that collagen levels in the tissue of nulliparous premenopausal women with SUI are lower than in those without UI (Keane et al., 1997). Collagen is an important fibrous protein which provides strength and elasticity, and is mainly located in the connective tissues (DeLancey & Starr, 1990). Ulmsten, Ekman, Giertz, and Malmstrom (1987) found that women with SUI had a 40% lower total concentration of hydroxyproline (the fundamental component of collagen) in the rectus fascia compared to continent women. Abnormal collagen can affect connective tissue, and consequently SUI could occur because the reduction in collagen weakens the paraurethral support (Falconer, Ekman, Malmström, & Ulmsten, 1994; Keane et al., 1997). The combination of the transmitted large forces with the lower collagen levels makes the pelvic floor more vulnerable to SUI.