Review: mapping proteins localized in adhesive setae of the tokay gecko and their possible influence on the mechanism of adhesion

Protoplasma. 2018 Nov;255(6):1785-1797. doi: 10.1007/s00709-018-1270-9. Epub 2018 Jun 7.

Abstract

The digital adhesive pads that allow gecko lizards to climb vertical surfaces result from the modification of the oberhautchen layer of the epidermis in normal scales. This produces sticky filaments of 10-100 μm in length, called setae that are composed of various proteins. The prevalent types, termed corneous beta proteins (CBPs), have a low molecular weight (12-20 kDa) and contain a conserved central region of 34 amino acids with a beta-conformation. This determines their polymerization into long beta-filaments that aggregate into corneous beta-bundles that form the framework of setae. Previous studies showed that the prevalent CBPs in the setae of Gekko gecko are cysteine-rich and are distributed from the base to the tip of adhesive setae, called spatulae. The molecular analysis of these proteins, although the three-dimensional structure remains undetermined, indicates that most of them are charged positively and some contain aromatic amino acids. These characteristics may impede adhesion by causing the setae to stick together but may also potentiate the van der Waals interactions responsible for most of the adhesion process on hydrophobic or hydrophilic substrates. The review stresses that not only the nanostructural shape and the high number of setae present in adhesive pads but also the protein composition of setae influence the strength of adhesion to almost any type of substrate. Therefore, formulation of dry materials mimicking gecko adhesiveness should also consider the chemical nature of the polymers utilized to fabricate the future dry adhesives in order to obtain the highest performance.

Keywords: Adhesive pads; Gecko lizard; Immunolocalization; Protein composition; Setae.

Publication types

  • Review

MeSH terms

  • Adhesiveness
  • Animals
  • Lizards
  • Proteins / chemistry*

Substances

  • Proteins