| Titre : |
Effect of hydrophilic or hydrophobic interactions on the self-assembly behavior and micro-morphology of a collagen mimetic peptide |
| Type de document : |
texte imprimé |
| Auteurs : |
Xiaomin Luo, Auteur ; Qianqian Huo, Auteur ; Liu Xinhua, Auteur ; Chi Zheng, Auteur ; Ying Liu, Auteur |
| Année de publication : |
2021 |
| Article en page(s) : |
10 p. |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Chimie biomimétique
Collagène
Dynamique moléculaire
Hydrophilie
Hydrophobie
Morphologie (matériaux)
Peptides
Systèmes auto-assemblés
|
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
Peptide self-assembles with bionic properties have been widely utilized for bioactive drugs and biomedical materials. Collagen mimetic peptide (CMP) gains more attention due to its unique advantages in biosecurity and function. Unfortunately, the self-assembly mechanism of CMP, particularly the effect of intermolecular forces on its self-assembly behavior and morphology, is still unrecognized. Herein, the hydrophilic glycidol (GCD) and hydrophobic Y-glycidyl ether oxypropyl trimethoxysilane (GLH) were grafted onto the side chains of CMP through the ring-opening reaction (GCD/CMP, GLH/CMP). Subsequently, the effects of hydrophilic and hydrophobic interactions on the self-assembly behavior and morphology of CMP were further studied. The results substantiated that the GCD/CMP and GLH/CMP self-assembly followed “nucleation-growth” mechanism, and the supererogatory hydrophilic and hydrophobic groups prolonged the nucleation and growth time of CMP self-assembly. Noted that the hydrophilic interaction had stronger driving effects than hydrophobic interaction on the self-assembly of CMP. The GCD/CMP and GLH/CMP self-assembles exhibited fibrous 3D network and microsphere morphology, respectively. Furthermore, the GLH/CMP self-assembles had better resistance to degradation. Consequently, the microtopography and degradation properties of CMP self-assembles could be controlled by the hydrophilic and hydrophobic interactions between CMP, which would further provide a way for subsequent purposeful design of biomedical materials. |
| Note de contenu : |
- EXPERIMENTS : Materials - Preparation of GCD/CMP, GLH/CMP and their homologous assemblies - Structural characterization of GCD/CMP, GLH/CMP - Self-assembly kinetics of GCD/CMP and GLH/CMP assemblies - Mico-morphology analysis of GCD/CMP and GLH/CMP assemblies - Performance characterization of GCD/CMP and GLH/CMP assemblies
- RESULTS AND DISCUSSION : Preparation and structural analysis of GCD/CMP and GLH/CMP - The self-assembly behavior of CMP, GCD/CMP and GLH/CMP - Performance analysis of CMP, GCD/CMP and GLH/CMP assemblies
- Table 1 Self-assembly rates of CMP, GCD/CMP and GLH/CMP |
| DOI : |
https://doi.org/10.1186/s42825-020-00054-3 |
| En ligne : |
https://link.springer.com/content/pdf/10.1186/s42825-021-00054-3.pdf |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37476 |
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 3 (Année 2021) . - 10 p.
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Effect of hydrophilic or hydrophobic interactions on the self-assembly behavior and micro-morphology of a collagen mimetic peptide in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 3 (Année 2021)
