DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2018-08-21 - Colloque/Présentation - poster - Anglais - 1 page(s)

Lefevre Mathilde , Flammang Patrick , Tafforeau Lionel , Wattiez Ruddy , Hennebert Elise , Leclère Philippe , "Production of biomimetic sea star adhesive proteins and characterization of their mechanical properties by scanning probe microscopy" in International Conference on Scanning Probe Microscopy on Soft and Polymeric Materials (SPMonSPM 2018) , Leuven, Belgium, 2018

  • Codes CREF : Biologie (DI3100)
  • Unités de recherche UMONS : Chimie des matériaux nouveaux (S817), Protéomie et Microbiologie (S828), Biologie des Organismes Marins et Biomimétisme (S864), Biologie cellulaire (S815)
  • Instituts UMONS : Institut de Recherche en Science et Ingénierie des Matériaux (Matériaux), Institut des Biosciences (Biosciences)

Abstract(s) :

(Anglais) Biological adhesives often offer impressive performance in their natural context and, therewith, the potential to inspire novel adhesives for an increasing variety of applications in medicine or in material sciences. Sea stars represent an interesting model for the study of marine adhesion. Indeed, they can attach strongly but temporarily to a variety of substrata using a multitude of small appendages, the tube feet. After the tube foot has become detached, the adhesive material, which appears as a fibrous meshwork-reinforced hydrogel, remains firmly bound to the substratum as a footprint [1,2]. Recently, transcriptome analysis and proteome analysis were combined to obtain sequences for all footprint-specific proteins [3]. Among these 35 proteins, 20 share similarities with known proteins but 15 others, within the most abundant in the secreted adhesive, remain unidentified. One of the adhesive proteins, the sea star footprint protein-1 (Sfp1, Figure 2) was characterized [4]. It is a major structural protein involved in footprint cohesion and possibly in adhesive interactions with the tube foot surface. The goal of this research project is to produce recombinant proteins based on the sequence of Sfp1. Some parts of this protein have been already produced: C-terminal part of subunit Beta, Delta subunit, and N-terminal and C-terminal part of Delta subunit (Figure 2). In a second time, these proteins will be characterized with an emphasis on functional characteristics such as adhesive properties, deformation and rigidity by AFM which is indeed an appropriate technique to visualize the microstructure, combined with the probing of the micromechanical properties of material surface in particular with Peak Force Tapping mode.