Potential Modulatory Effects of β-Hydroxy-β-Methylbutyrate on Type I Collagen Fibrillogenesis: Preliminary Study
Artykuł w czasopiśmie
MNiSW
140
Lista 2024
| Status: | |
| Autorzy: | Świetlicka Izabela, Janek Eliza, Gołacki Krzysztof, Krakowiak Dominika, Świetlicki Michał, Arczewska Marta |
| Dyscypliny: | |
| Aby zobaczyć szczegóły należy się zalogować. | |
| Rok wydania: | 2025 |
| Wersja dokumentu: | Drukowana | Elektroniczna |
| Język: | angielski |
| Numer czasopisma: | 19 |
| Wolumen/Tom: | 26 |
| Numer artykułu: | 9621 |
| Strony: | 1 - 17 |
| Impact Factor: | 4,9 |
| Web of Science® Times Cited: | 0 |
| Scopus® Cytowania: | 0 |
| Bazy: | Web of Science | Scopus |
| Efekt badań statutowych | NIE |
| Materiał konferencyjny: | NIE |
| Publikacja OA: | TAK |
| Licencja: | |
| Sposób udostępnienia: | Witryna wydawcy |
| Wersja tekstu: | Ostateczna wersja opublikowana |
| Czas opublikowania: | W momencie opublikowania |
| Data opublikowania w OA: | 2 października 2025 |
| Abstrakty: | angielski |
| β-Hydroxy-β-methylbutyrate (HMB), a natural metabolite derived from the essential amino acid leucine, is primarily recognised for its anabolic and anti-catabolic effects on skeletal muscle tissue. Recent studies indicate that HMB may also play a role in influencing the structural organisation of extracellular matrix (ECM) components, particularly collagen, which is crucial for maintaining the mechanical integrity of connective tissues. In this investigation, bovine type I collagen was polymerised in the presence of two concentrations of HMB (0.025 M and 0.25 M) to explore its potential function as a molecular modulator of fibrillogenesis. The morphology of the resulting collagen fibres and their molecular architecture were examined using atomic force microscopy (AFM) and Fourier-transform infrared (FTIR) spectroscopy. The findings demonstrated that lower levels of HMB fa- cilitated the formation of more regular and well-organised fibrillar structures, exhibiting increased D-band periodicity and enhanced stabilisation of the native collagen triple he- lix, as indicated by Amide I and III band profiles. Conversely, higher concentrations of HMB led to significant disruption of fibril morphology and alterations in secondary struc- ture, suggesting that HMB interferes with the self-assembly of collagen monomers. These structural changes are consistent with a non-covalent influence on interchain interactions and fibril organisation, to which hydrogen bonding and short-range electrostatics may contribute. Collectively, the results highlight the potential of HMB as a small-molecule regulator for soft-tissue matrix engineering, extending its consideration beyond metabolic supplementation towards controllable, materials-oriented modulation of ECM structure. |
