Self-assembling of chimeric mussel-inspired bio-adhesives originated from Mytilus californianus and Anabaena flos-aquae: A new approach to develop underwater adhesion

Hamidreza Iranpour,Sareh Zhand,Mahdi Mohammadi Ghanbarlu,Hani Hosseini Far,Seyed Nezamedin Hosseini,Saeid Bouzari,Mohammad Ali Shokrgozar,Hosein Shahsavarani

doi:10.1016/j.ijadhadh.2021.102938

Abstract

Bio-adhesives play a pivotal role in a wide range of medical applications. However, there are some problems about their application in different pH values and low adhesion force under wet conditions. Here, we report new recombinant fusion protein achieved by mussel foot proteins (Mfps) of Mytilus Californianus and gas vesicle protein A (GvpA) of Anabaena flos-aquae by genetic engineering methods. Transmission electron microscopy verified that these chimeric proteins self-assembled into β-sheet rich fibres because of GvpA amyloid structure. Also, in comparison to other studies, their adhesion forces were significantly increased, especially in the alkaline environments based on Mfp-3 and Mfp-5, confirmed by the colloidal probe atomic force microscope. This study illustrates that copolymer of Mfp-5-GvpA:GvpA-Mfp-3 can be used as a sturdy underwater adhesive with tolerance to auto-oxidation, especially at basic conditions.

Highlights

Bio-inspired adhesives originated from mussel, barnacles, Notaden frogs and gecko have had extensive interest among scientists due to being water-based adhesive[1,2,3,4,5]
E. coli BL21-AI have been used as alternative for resolving this problem[19,20]
Most of the recombinant proteins were expressed as inclusion body (IB) in E. coli

Summary

Introduction

Bio-inspired adhesives originated from mussel, barnacles, Notaden frogs and gecko have had extensive interest among scientists due to being water-based adhesive[1,2,3,4,5]. After purification with nickel-IDA agarose 6% under danturated conditions (Figure 5), concentration of purified proteins was obtained at 0.7439 (mg/mL) and 0.8937 (mg/ml) for Mfp-5-GvpA and Mfp-3-GvpA proteins through the BCA Protein Assay, respectively. Modification and confirmation of recombinant protein with tyrosinase treatment qualitatively and quantitatively: In order to obtain adhesive features, tyrosinase was added to purified proteins (unmodified Mfp5-GvpA and unmodified Mpf-3-GvpA).

Results

Conclusion