دورية أكاديمية
Deepening in the understanding of the role of collagen subunits on the differential molecular arrangement of P. glauca and M. merluccius marine collagens
| العنوان: | Deepening in the understanding of the role of collagen subunits on the differential molecular arrangement of P. glauca and M. merluccius marine collagens |
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| المؤلفون: | Blanco Comesaña, M., Sanz Pereira, Noelia, Pérez Martín, Ricardo Isaac, González Sotelo, Carmen |
| المساهمون: | European Commission, Xunta de Galicia |
| بيانات النشر: | Elsevier |
| سنة النشر: | 2023 |
| المجموعة: | Digital.CSIC (Consejo Superior de Investigaciones Científicas / Spanish National Research Council) |
| مصطلحات موضوعية: | Collagen fibres, Collagen subunits, Intermolecular crosslink, α2-chain dimerization, Collagen supramolecular assembly |
| الوصف: | 10 pages, 11 figures, 1 table.-- Under a Creative Commons license ; Decades of extensive efforts on marine collagen extraction and characterization allowed to recognize the unique and excellent characteristics of marine collagen offering advantages over that obtained from terrestrial sources. However, not all marine collagens have the same biochemical characteristics; understanding those at molecular and supramolecular level, is crucial for optimal design of applications. One relevant aspect of collagen characterization is the analysis of its different subunits (α-chains) and their intermolecular cross-links (β- and γ-components), which ultimately determine the specific functions of a particular collagen. Collagens from a teleost and an elasmobranch species were analyzed to understand the influence of their subunit composition and intermolecular crosslinking pattern on their different physicochemical behaviour. For comparative purposes a commercial mammal collagen was included in the study. Although electrophoretic profiles showed the typical composition of type I collagen for hake, blue shark and calf collagen, molar ratios of their α-chains were different indicating a different degree of dimerization of their α2-chains with implications in the presence of a different crosslinking degree pattern. Electrophoresis, amino acid composition, hydrophobicity (RP-HPLC) and molecular weight analysis (GPC-HPLC) results, besides a peptide mapping and an antioxidant activity study of the resultant peptides, would help to understand the role of different subunit collagen composition and different crosslinking pattern in the conformation of a differential quaternary supramolecular structure within different species and its biofunctional implications. The experiments developed would allow to progress in the valorization potential of fish discards and byproducts to explore commercial uses of collagens from marine origin ; This research was funded by project BlueHuman (EU EAPA151/2016) and Xunta de Galicia (Grupos de Potencial ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1046-5928 |
| العلاقة: | Publisher's version; Data will be made available on request; https://doi.org/10.1016/j.pep.2023.106356Test; Sí; Protein Expression and Purification 212: 106356 (2023); http://hdl.handle.net/10261/334863Test |
| DOI: | 10.1016/j.pep.2023.106356 |
| الإتاحة: | https://doi.org/10.1016/j.pep.2023.106356Test http://hdl.handle.net/10261/334863Test |
| حقوق: | open |
| رقم الانضمام: | edsbas.5C6E8473 |
| قاعدة البيانات: | BASE |
| تدمد: | 10465928 |
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| DOI: | 10.1016/j.pep.2023.106356 |