Utilization of Fisheries' By-Products for Functional Foods
Se-Kwon Kim in Marine Biochemistry, 2023
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
Chuong Pham-Huy, Bruno Pham Huy in Food and Lifestyle in Health and Disease, 2022
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.
Lactic Acid Bacteria Application to Decrease Food Allergies
Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani in Lactic Acid Bacteria, 2020
In the case of amino acids, at least 10 different transport systems, with high specificity, have been identified in lactococci and lactobacilli. These systems can be regulated by ATP hydrolysis (for Glu/Gln, Asn, and Pro/Gly), by proton motive force (PMF for Leu/Val/Ile, Ala/Gly, Ser/Thr, and Met) or by passive transport based on the concentration gradient (for Arg/Orn). The transport of di- and tripeptides is similar to that of essential amino acids. The mechanism is regulated by PMF-driven DtpT and ATP-driven Dpp enzymes, which require proton generation and ATP hydrolysis, respectively. Dpp enzymes allow the transport of di- and tripeptides containing relatively hydrophobic branched-chain amino acids, with higher affinity to tripeptides, while DtpT enzymes present a preference for more hydrophilic and charged di- and tripeptides. Oligopeptides are carried through the cell membrane by enzymes belonging to the ABC family. This system consists of five proteins (Opp A, B, C, D, and F), belonging to a super family of highly conserved ATP-dependent cassette transporters. These proteins can carry oligopeptides containing up to at least 18 residues and the transport kinetics are affected by the nature of peptides been carried. Although the Opp system is well characterized for L. lactis, some authors mention that these transporters are similar for other LAB, such as Lactobacillus spp. and Streptococcus spp. (Savijoki et al. 2006, Rodríguez-Serrano et al. 2018).
Topical application of sh-oligopeptide-1 and clinical trials with cosmetic preparations: risk or fraud?
Published in Cutaneous and Ocular Toxicology, 2023
The commercial contents of the websites of all the manufacturers reflect a lack of referenced scientific information on the molecular and functional characteristics of the oligopeptide. They all state, as a marketing strategy, that it is a molecule that contains the same sequence of 53 amino acids and performs the same functions as human EGF, with no valid scientific demonstration. They use different types of plant cells, especially barley and Nicotiana benthamiana, and different recombinant synthesis techniques, but without demonstrating a functional tertiary structure. Each manufacturer defends the characteristics that set their sh-oligopeptide-1 apart from that of their market competitors. They all assure that sh-oligopeptide-1 is a molecule with identical or similar functions to EGF. The products are marketed under the name EGF, not sh-oligopeptide-1, which only appears in the formula of the product, without specifying the concentration. The cosmetic products are not authorised to include EGF in their composition, because it is different from sh-oligopeptide-1. The term EGF is reserved for the name of the product, leading to a misleading interpretation of a commercial nature.
Targeting protein-protein interactions with low molecular weight and short peptide modulators: insights on disease pathways and starting points for drug discovery
Published in Expert Opinion on Drug Discovery, 2023
Daniela Trisciuzzi, Bruno O. Villoutreix, Lydia Siragusa, Massimo Baroni, Gabriele Cruciani, Orazio Nicolotti
In a recent innovative study, a statistical analysis of the most frequent polar and hydrophobic residue pairs occurring at peptide-protein interaction sites was integrated with deep energetic investigations based on a GRID molecular interaction fields (GRID-MIFs) aiming to assess the chance of finding complementary groups at peptide-protein interface [169]. The leucine-leucine hydrophobic pairing was the more frequently observed at the peptide-protein interface [170]. Conversely, the most occurring polar pairing was given by the glutamate-arginine, on target and peptide sides, respectively (Figure 5). The analysis highlighted the potential of the GRID strategy to structurally and energetically characterize the oligopeptide recognition sites by quantifying the strength of interactions that a given peptide (and vice versa the target) can establish.
Evaluation of GHK peptide–heparin interactions in multifunctional liposomal covering
Published in Journal of Liposome Research, 2023
Viktoriia Nikolaeva, Marat Kamalov, Timur I. Abdullin, Diana Salakhieva, Vitaly Chasov, Alexey Rogov, Mohamed Zoughaib
Effective surface modification of liposomes with biospecific agents represents a relevant task to elaborate vesicular systems for both fundamental membrane research and targeted drug delivery applications (Filipczak et al.2020, Wang et al.2021). Antibodies, enzymes, aptamers, metabolites and peptides have been investigated as modifying agents for liposomes (Khan et al.2020). Short peptide sequences, i.e. oligopeptides (OPs), primarily derived from functional sites of natural polypeptides, hold particular promises owing to their stability and low immunogenicity compared to full-length proteins (Vlieghe et al.2010, Visser et al.2016, Gomes et al.2017). OPs can endow liposomal formulations with affinity to membrane receptors and ability to penetrate the cells and induce specific intracellular responses (Yang et al.2015). Established chemical methods such as solid phase peptide synthesis (SPPS) allow the production of required peptide sequences and their modification with non-canonical moieties to alter biological properties (e.g. proteolytic resistance) and mediate binding to liposomes (Palomo 2014). The state of the art in using cell-targeting OPs for drug delivery is summarised in recent reviews (Accardo and Morelli 2015, Cheng and Ji 2019, Jiang et al.2019).
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