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Utilization of Fisheries' By-Products for Functional Foods
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Muhamad Darmawan, Nurrahmi Dewi Fajarningsih, Sihono, Hari Eko Irianto
The antimicrobial activities of gelatin depend on their sequence of peptides, amino acid composition, hydrophobicity, attributes of molecular weight, and charge state (Kouhdasht et al., 2021). Gelatin from salmon showed antimicrobial activities due to its oligopeptide content that is obtained during the extraction of gelatin from salmon skin collagen. Oligopeptides, short peptides built of 2–10 residues of amino acid with less than 1 kDa molecular weight, have been reported to exhibit antimicrobial activity (Gomez-Guillen et al., 2010; Matiacevich et al., 2013; Wang et al., 2018). Additionally, the ability of collagen to penetrate a lipid-free interface and easily absorbable make it has fungicidal and bactericidal properties, low antigenicity and superior biocompatibility. According to those attributes, collagen could be used as a good surface-active agent (Jus et al., 2009). The biodegradable films and active packaging materials can be formulated by enriching the gelatin films with natural antioxidant or antimicrobial substances (Kavoosi et al., 2013; Kim and Mendis, 2006).
Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
In cells, a peptide is formed when two adjacent amino acids are linked together through the carboxyl (COOH) group of one amino acid with the amino (NH2) group of another to form an amide bond (-CONH-), also called peptide bond. The chain, thus formed, by linking together of many amino acid units is called a peptide chain (36, 38, 41). The two amino acids at the ends of the chain are called N-terminal and C-terminal where the groups NH2 and COOH are not linked – free or intact. Depending on the number of amino acid molecules composing a chain, the peptides may be termed as a dipeptide (containing 2 amino acid units), a tripeptide (containing 3 amino acid units) and so on. If a peptide is made up of no more than ten amino acids, it is called an oligopeptide; beyond that, it is a polypeptide. Peptide chain may possess from 50 to millions of amino acid units. When they are made up of over 100 amino acids, polypepties are sometimes called macro-peptides. Strictly speaking, proteins are polypeptides with more than 100 amino acids (38). However, this classification is arbitrary, and the number of amino acids can vary according to each author.
Mass Spectrometric Analysis
Published in Adorjan Aszalos, Modern Analysis of Antibiotics, 2020
The primary advantage of desorption CI is its simplicity. This is reflected in its cost and ease of adapting to any instruments with a CI source. Good results have been obtained from nonvolatile and labile compounds not amenable to conventional methods. These include carbohydrates, oligopeptides and organic salts. The spectra typically show (M + H)+ ions with varying amounts of fragmentation ions.
3D self-assembled nanocarriers for drug delivery
Published in Drug Metabolism Reviews, 2023
Hossein Karballaei Mirzahosseini, Mojgan Sheikhi, Farhad Najmeddin, Mehrnoosh Shirangi, Mojtaba Mojtahedzadeh
The development of peptides is a smaller part of many attempts to create biomaterials and drugs utilizing supramolecular chemistry (Webber et al. 2016). Peptide self-assembly offers several advantages when used to create medicinal compounds. These include the possibility to produce medications tailored to a patient’s needs or a particular illness by creating modular platforms from the simultaneous co-assembly of many peptides. The materials that form differ often from conventional polymeric biomaterials in their capacity to respond to stimuli more quickly through dynamic and reversible changes in their characteristics because self-assembly is based on noncovalent forces. The dispersity of polymeric and other soft material building blocks contrasts with their simplicity of synthesis, and nonpeptidic groups can also be added to peptides during synthesis (e.g. drugs, polymers, and lipids). Therefore, oligopeptide assembly offers a number of beneficial advantages for developing novel drug delivery materials.
The development of inovirus-associated vector vaccines using phage-display technologies
Published in Expert Review of Vaccines, 2019
Zachariah Stern, Dora C. Stylianou, Leondios G. Kostrikis
Inoviruses are useful for vaccine development because it is possible to insert random oligonucleotides into their genome. This easy genetic manipulation is the basis for inovirus display (phage display) technology [32,33]. Inoviruses that have been genetically modified to display these oligopeptides as fusion proteins on their surface are referred to as inovirus-associated vectors (IAVs). Oligopeptides can be displayed on any capsid protein (gp3, gp6, gp7, gp8, and gp9) following genetic modification. A specific oligonucleotide sequence can be inserted into the viral genome to display the desired oligopeptide as a fusion with capsid proteins gp3, gp7, gp8, or gp9. This results in the oligopeptide’s display on every copy of the target capsid protein. However, mosaic inovirus particles can be created where the specific capsid proteins display a mix of wild type and recombinant proteins with the desired oligopeptide [34]. This is done using a phagemid vector which has an extra copy of a capsid protein fused to the specific oligonucleotide. A host exposed to both the phagemid vector and a wild type capsid protein from a deficient helper phage produces mosaic IAVs displaying both wild type and oligopeptide fused capsid proteins. Work using the capsid protein gp6 has resulted only in the production of mosaic IAVs (for reviews see [35–37]) while both mosaic and non-mosaic IAVs have been produced using gp3 and gp8 (for a review see [10]) and gp7 and gp9 (for reviews see [38–40]).
An assessment of the translational relevance of Drosophila in drug discovery
Published in Expert Opinion on Drug Discovery, 2019
Katerina Papanikolopoulou, Amrit Mudher, Efthimios Skoulakis
Drug efficacy in a relevant Drosophila model could provide the initial step towards testing rationally modified compounds in an animal model. For example, the microtubule stabilizing oligopeptide drug Davunetide used in various mammalian models of neurological disorders with variable results [119], has also been demonstrated active in a fly Tauopathy model [8], enabling a better understanding of its mode of action. Significantly, this provides an entry point for expedient testing of rational modifications that may improve the efficacy of this oligopeptide. In a similar approach, the in vivo efficacy of the Ret kinase inhibitor Vandetanib was assessed and was found to present low toxicity and high efficacy in ameliorating the aberrant eye phenotype of flies overexpressing therein the constitutively active kinase [120]. This is likely beneficial for patients with Ret activation–linked hereditary medullary thyroid carcinoma and radiation or chemotherapy are ineffective.