Recombinant lubricin improves anti-adhesive, wear protection, and lubrication of collagen II surface

Hui Yuan; Laura L E Mears; Xiao Liu; Wei Qi; Rongxin Su; Markus Valtiner

doi:10.1016/j.colsurfb.2022.112906

Recombinant lubricin improves anti-adhesive, wear protection, and lubrication of collagen II surface

Colloids Surf B Biointerfaces. 2022 Dec:220:112906. doi: 10.1016/j.colsurfb.2022.112906. Epub 2022 Oct 10.

Authors

Hui Yuan¹, Laura L E Mears², Xiao Liu³, Wei Qi³, Rongxin Su⁴, Markus Valtiner⁵

Affiliations

¹ State Key Laboratory of Chemical Engineering, Tianjin Key Laboratory of Membrane Science and Desalination Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; Institute of Applied Physics, Vienna University of Technology, Vienna 1040, Austria.
² Institute of Applied Physics, Vienna University of Technology, Vienna 1040, Austria.
³ State Key Laboratory of Chemical Engineering, Tianjin Key Laboratory of Membrane Science and Desalination Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
⁴ State Key Laboratory of Chemical Engineering, Tianjin Key Laboratory of Membrane Science and Desalination Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; School of Marine Science and Technology, Tianjin University, Tianjin 300072, China. Electronic address: surx@tju.edu.cn.
⁵ Institute of Applied Physics, Vienna University of Technology, Vienna 1040, Austria. Electronic address: markus.valtiner@tuwien.ac.at.

PMID: 36252540
DOI: 10.1016/j.colsurfb.2022.112906

Abstract

Camptodactyly-arthropathy-coxa vara-pericarditis syndrome (CACP) is a joint disease caused by a lack of lubricin, resulting in failed lubrication and abnormal deposition at the cartilage surface. Injection of recombinant lubricin (R-LUB) is a promising approach to improve the symptoms of the disease. However, the antifouling and lubrication properties of R-LUB on cartilage surfaces have not yet been studied. Here, the adsorption and lubrication behavior of a type II collagen (COL II) mimicking the cartilage surface upon R-LUB injection was followed by surface plasmon resonance spectroscopy and surface forces apparatus. The results indicated R-LUB can bind well on a COL II surface and COL II/R-LUB complex layer exhibited ultralow nonspecific adsorption of BSA (3.25 ng/cm²) and LYS (0.26 ng/cm²) compared to those of the COL II layer (32.7 ng/cm², 7.26 ng/cm²). Normal force measurements indicated there was always a repulsive force between COL II/R-LUB complex and different surfaces with -COO^-, -NH₃^+, and -CH₃ groups. Likewise, COL II had a high coefficient of friction (∼0.48) with surface damage at 2 µm/s and a wear pressure of 1.56 MPa, while that of COL II/R-LUB complex was down to ∼0.008-0.13 with surface damage at 13 µm/s and a wear pressure of 11.96 MPa, which was 7.7 times higher than for COL II. Hence, R-LUB may act as an anti-adhesive and lubrication layer adsorbed on COL II surfaces to prevent direct contact. Our findings provide fundamental insights into the adsorption and lubrication behavior for understanding biological lubrication, especially the potential supplementation of R-LUB for treating CACP disease.

Keywords: Antiadhesive; Collagen II; Lubrication; Recombinant lubricin; Wear protection.

MeSH terms

Adhesives*
Collagen*
Friction
Lubrication
Surface Properties

Substances

lubricin
Adhesives
Collagen